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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0514 [new locus tag: SACOL_RS02595 ]
- pan locus tag?: SAUPAN002186000
- symbol: gltB
- pan gene symbol?: gltB
- synonym:
- product: glutamate synthase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0514 [new locus tag: SACOL_RS02595 ]
- symbol: gltB
- product: glutamate synthase
- replicon: chromosome
- strand: +
- coordinates: 513658..518157
- length: 4500
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237089 NCBI
- RefSeq: YP_185402 NCBI
- BioCyc: see SACOL_RS02595
- MicrobesOnline: 911982 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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4441ATGCACAATGAGAAATTAATTAAAGGCTTATATGACTATCGTGAGGAACATGATGCGTGT
GGTATTGGTTTTTATGCGAATATGGATAATAAAAGGTCTCACGACATCATTGATAAATCG
CTTGAAATGTTGCGACGCTTAGATCACAGGGGCGGGGTCGGCGCAGATGGCATCACTGGT
GATGGCGCAGGTATTATGACTGAAATACCTTTTGCATTTTTCAAACAACATGTAACGGAC
TTTGATATCCCAGGTGAAGGTGAATATGCCGTGGGGTTATTTTTTTCCAAAGAACGCATT
TTAGGTTCTGAACATGAAGTAGTTTTTAAAAAATATTTTGAAGGCGAAGGGTTATCAATT
CTTGGTTATCGTAATGTACCAGTTAATAAAGATGCCATTGCTAAACATGTAGCAGATACG
ATGCCAGTCATTCAACAAGTGTTTATTGATATTAGGGACATTGAAGATGTTGAAAAGCGT
TTGTTTTTAGCGAGAAAACAATTAGAGTTCTATTCGACTCAGTGCGATTTAGAATTGTAT
TTTACGAGCTTATCACGCAAAACAATTGTATATAAAGGTTGGTTACGATCAGACCAAATT
AAAAAAGTATATACAGATTTATCGGATGATTTATATCAATCAAAGCTAGGGTTAGTGCAT
TCGAGATTTAGTACGAATACATTCCCGAGTTGGAAAAGGGCACATCCTAACCGTATGTTA
ATGCATAATGGTGAGATTAACACGATTAAAGGTAATGTAAACTGGATGCGAGCACGCCAA
CATAAATTAATCGAAACATTATTTGGCGAGGATCAACATAAAGTGTTTCAAATTGTCGAT
GAGGATGGTAGTGACTCTGCCATTGTAGATAATGCGCTAGAGTTCTTATCGTTAGCCATG
GAGCCAGAAAAGGCAGCGATGTTACTCATACCTGAACCTTGGTTATATAATGAAGCGAAT
GATGCAAATGTACGTGCGTTTTATGAATTTTATAGTTATTTAATGGAACCGTGGGATGGT
CCTACAATGATTTCGTTCTGTAACGGTGACAAACTTGGCGCGCTTACAGATAGAAATGGA
TTACGTCCAGGTCGTTATACGATTACTAAAGATAACTTTATTGTCTTTTCATCTGAAGTG
GGTGTTGTGGACGTACCTGAAAGTAATGTTGCTTTTAAAGGTCAATTGAATCCTGGAAAG
TTATTGCTTGTTGATTTTAAACAGAATAAAGTCATTGAAAATAATGATTTAAAAGGTGCG
ATTGCTGGAGAATTACCATATAAAGCGTGGATTGATAACCATAAAGTTGACTTTGATTTT
GAAAATATACAATATCAAGATTCGCAATGGAAAGATGAGACGTTATTTAAATTACAACGT
CAGTTTGCATACACGAAAGAAGAGATTCATAAGTATATTCAGGAACTTGTAGAAGGTAAG
AAGGATCCTATCGGTGCAATGGGATATGATGCGCCAATTGCAGTGTTGAACGAGCGACCA
GAATCACTATTTAATTACTTTAAACAGCTGTTTGCACAAGTTACGAATCCACCAATTGAT
GCGTATCGTGAAAAAATCGTAACGAGTGAACTTTCTTATTTAGGTGGCGAAGGTAACTTA
CTAGCACCTGACGAAACGGTTTTAGATCGTATTCAATTGAAAAGGCCGGTATTGAATGAA
TCACACTTAGCAGCGATTGATCAGGAACATTTTAAATTAACTTATTTATCAACGGTATAT
GAAGGGGATTTGGAAGATGCGTTAGAAGCATTAGGCCGAGAAGCAGTGAATGCTGTAAAG
CAAGGCGCTCAAATTCTAGTGTTAGATGATAGTGGATTAGTTGATAGCAATGGCTTTGCA
ATGCCGATGTTACTCGCAATAAGTCATGTGCATCAATTACTTATTAAAGCAGATTTACGT
ATGTCTACAAGTTTAGTCGCTAAATCTGGTGAGACACGAGAAGTGCATCATGTTGCTTGT
TTACTCGCATATGGCGCGAATGCAATTGTGCCATACCTAGCGCAACGTACAGTTGAACAA
CTGACATTGACAGAAGGGTTACAAGGCACCGTTGTCGATAATGTTAAGACATATACGGAT
GTATTGTCAGAAGGTGTCATTAAAGTAATGGCTAAGATGGGAATTTCGACAGTGCAAAGT
TATCAAGGGGCACAAATATTTGAAGCGATTGGCTTGTCTCATGATGTGATTGATCGTTAT
TTTACTGGGACACAGTCTAAGTTATCTGGTATTTCGATTGATCAAATTGATGCTGAAAAT
AAAGCACGTCAACAAAGTGATGATAATTATCTTGCATCAGGTAGTACATTCCAATGGAGA
CAACAAGGTCAACATCATGCTTTTAATCCGGAATCTATTTTCTTATTGCAGCACGCATGT
AAAGAAAATGACTATGCGCAATTTAAAGCATACTCTGAAGCGGTGAACAAAAATAGAACA
GATCACATTAGACATTTACTTGAATTTAAAGCATGTACACCGATTGACATCGACCAAGTT
GAACCGGTAAGTGACATTGTCAAACGCTTTAATACAGGGGCGATGAGTTATGGATCGATT
TCAGCGGAAGCACATGAAACGTTAGCACAAGCCATGAACCAATTAGGTGGAAAGAGTAAT
AGTGGTGAAGGTGGCGAAGATGCAAAACGTTATGAAGTACAAGTTGATGGAAGCAACAAA
GTAAGTGCGATTAAACAAGTTGCTTCTGGGCGTTTTGGTGTAACTAGTGATTATTTACAA
CATGCCAAAGAAATTCAAATTAAAGTTGCGCAAGGTGCAAAGCCTGGTGAAGGTGGTCAA
TTACCTGGTACTAAGGTATATCCGTGGATTGCGAAGACAAGAGGGTCAACGCCAGGTATC
GGTCTGATTTCACCACCGCCACATCATGATATTTATTCAATAGAAGATTTAGCGCAACTG
ATACATGATTTGAAAAATGCGAATAAAGATGCAGATATCGCGGTAAAATTAGTTTCGAAA
ACAGGTGTTGGTACCATTGCATCTGGGGTGGCAAAAGCATTTGCAGATAAAATTGTCATC
AGTGGTTACGATGGTGGTACAGGGGCTTCACCCAAAACGAGTATTCAGCATGCCGGTGTT
CCTTGGGAGATTGGTTTAGCAGAAACACATCAAACATTAAAACTAAATGACTTAAGAAGT
CGTGTTAAGTTAGAAACAGACGGTAAGTTATTAACTGGTAAAGATGTAGCGTACGCATGT
GCGCTTGGAGCGGAAGAATTTGGATTTGCAACTGCACCATTAGTGGTGTTGGGCTGTATT
ATGATGCGTGTATGCCATAAAGATACATGTCCAGTAGGAGTTGCAACTCAAAACAAAGAT
TTACGTGCTTTATATAGAGGTAAAGCACATCATGTTGTTAATTTTATGCATTTTATTGCA
CAAGAATTAAGAGAAATTTTAGCATCTTTAGGTTTGAAACGTGTAGAAGACTTAGTTGGA
AGAACTGATTTATTACAACGATCATCAACATTAAAAGCGAATAGCAAAGCGGCTAGTATT
GATGTTGAAAAACTGTTATGTCCTTTCGATGGGCCAAACACAAAAGAAATTCAACAAAAT
CATAATCTTGAGCATGGATTTGATTTAACAAATTTATATGAAGTAACGAAGCCATATATT
GCTGAAGGGCGTCGCTATACAGGTAGCTTTACAGTAAATAATGAACAACGTGATGTAGGG
GTTATTACAGGTAGTGAGATTTCGAAACAATATGGAGAAGCAGGACTTCCTGAAAATACA
ATTAATGTTTATACGAATGGTCATGCTGGTCAAAGTCTTGCAGCATATGCACCGAAAGGC
TTAATGATTCATCATACTGGAGATGCGAATGACTATGTTGGTAAAGGATTATCTGGTGGT
ACGGTCATTGTCAAAGCACCTTTTGAAGAACGACAAAATGAAATTATTGCTGGTAACGTC
TCATTCTATGGTGCGACAAGTGGTAAGGCATTTATTAACGGTAGTGCAGGAGAAAGATTC
TGTATTAGAAATAGTGGTGTAGATGTTGTCGTTGAAGGTATCGGCGACCATGGATTAGAG
TATATGACTGGTGGACATGTCATTAATTTAGGTGATGTAGGTAAGAACTTCGGTCAAGGT
ATGAGTGGTGGTATTGCTTACGTTATCCCGTCTGATGTAGAAGCTTTTGTTGAAAATAAT
CAACTAGATACGCTTTCGTTTACAAAGATTAAACACCAAGAAGAAAAAGCATTCATTAAG
CAAATGCTGGAAGAACATGTGTCACACACGAATAGTACGAGAGCGATTCATGTGTTAAAA
CATTTTGATCGCATTGAAGATGTCGTCGTTAAAGTTATTCCTAAAGATTATCAATTAATG
ATGCAAAAAATTCATTTGCACAAATCATTACATGACAATGAAGATGAAGCGATGTTAGCT
GCATTTTACGATGACAGTAAAACAATCGATGCTAAACATAAACCAGCCGTTGTGTATTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0514 [new locus tag: SACOL_RS02595 ]
- symbol: GltB
- description: glutamate synthase
- length: 1499
- theoretical pI: 5.97235
- theoretical MW: 166333
- GRAVY: -0.315944
⊟Function[edit | edit source]
- reaction: EC 1.4.1.13? ExPASyGlutamate synthase (NADPH) 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH
- TIGRFAM: formylmethanofuran dehydrogenase subunit C (TIGR03122; EC 1.2.99.5; HMM-score: 25.9)
- TheSEED :
- Glutamate synthase [NADPH] large chain (EC 1.4.1.13)
Amino Acids and Derivatives Glutamine, glutamate, aspartate, asparagine; ammonia assimilation Glutamine, Glutamate, Aspartate and Asparagine Biosynthesis Glutamate synthase [NADPH] large chain (EC 1.4.1.13)and 1 more - PFAM: TIM_barrel (CL0036) Glu_synthase; Conserved region in glutamate synthase (PF01645; HMM-score: 521.3)NTN (CL0052) GATase_2; Glutamine amidotransferases class-II (PF00310; HMM-score: 513.7)and 3 moreTIM_barrel (CL0036) Glu_syn_central; Glutamate synthase central domain (PF04898; HMM-score: 330.4)no clan defined GXGXG; GXGXG motif (PF01493; HMM-score: 225.1)TIM_barrel (CL0036) FMN_dh; FMN-dependent dehydrogenase (PF01070; HMM-score: 9.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic Membrane
- Cytoplasmic Score: 1.78
- Cytoplasmic Membrane Score: 8.16
- Cellwall Score: 0.06
- Extracellular Score: 0.01
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.029572
- TAT(Tat/SPI): 0.000731
- LIPO(Sec/SPII): 0.001237
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MHNEKLIKGLYDYREEHDACGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTDFDIPGEGEYAVGLFFSKERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFIDIRDIEDVEKRLFLARKQLEFYSTQCDLELYFTSLSRKTIVYKGWLRSDQIKKVYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRMLMHNGEINTIKGNVNWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLAMEPEKAAMLLIPEPWLYNEANDANVRAFYEFYSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGKLLLVDFKQNKVIENNDLKGAIAGELPYKAWIDNHKVDFDFENIQYQDSQWKDETLFKLQRQFAYTKEEIHKYIQELVEGKKDPIGAMGYDAPIAVLNERPESLFNYFKQLFAQVTNPPIDAYREKIVTSELSYLGGEGNLLAPDETVLDRIQLKRPVLNESHLAAIDQEHFKLTYLSTVYEGDLEDALEALGREAVNAVKQGAQILVLDDSGLVDSNGFAMPMLLAISHVHQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQGTVVDNVKTYTDVLSEGVIKVMAKMGISTVQSYQGAQIFEAIGLSHDVIDRYFTGTQSKLSGISIDQIDAENKARQQSDDNYLASGSTFQWRQQGQHHAFNPESIFLLQHACKENDYAQFKAYSEAVNKNRTDHIRHLLEFKACTPIDIDQVEPVSDIVKRFNTGAMSYGSISAEAHETLAQAMNQLGGKSNSGEGGEDAKRYEVQVDGSNKVSAIKQVASGRFGVTSDYLQHAKEIQIKVAQGAKPGEGGQLPGTKVYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGVAKAFADKIVISGYDGGTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFATAPLVVLGCIMMRVCHKDTCPVGVATQNKDLRALYRGKAHHVVNFMHFIAQELREILASLGLKRVEDLVGRTDLLQRSSTLKANSKAASIDVEKLLCPFDGPNTKEIQQNHNLEHGFDLTNLYEVTKPYIAEGRRYTGSFTVNNEQRDVGVITGSEISKQYGEAGLPENTINVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIVKAPFEERQNEIIAGNVSFYGATSGKAFINGSAGERFCIRNSGVDVVVEGIGDHGLEYMTGGHVINLGDVGKNFGQGMSGGIAYVIPSDVEAFVENNQLDTLSFTKIKHQEEKAFIKQMLEEHVSHTNSTRAIHVLKHFDRIEDVVVKVIPKDYQLMMQKIHLHKSLHDNEDEAMLAAFYDDSKTIDAKHKPAVVY
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 210 [4]
- interaction partners:
SACOL1760 (ackA) acetate kinase [5] (data from MRSA252) SACOL2218 (adk) adenylate kinase [5] (data from MRSA252) SACOL1800 (dat) D-alanine aminotransferase [5] (data from MRSA252) SACOL2130 (deoD) purine nucleoside phosphorylase [5] (data from MRSA252) SACOL0937 (dltC) D-alanine--poly(phosphoribitol) ligase subunit 2 [5] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [5] (data from MRSA252) SACOL0988 (fabF) 3-oxoacyl-ACP synthase [5] (data from MRSA252) SACOL1245 (fabG1) 3-oxoacyl-ACP reductase [5] (data from MRSA252) SACOL1016 (fabI) enoyl-ACP reductase [5] (data from MRSA252) SACOL2117 (fbaA) fructose-bisphosphate aldolase [5] (data from MRSA252) SACOL2622 (fdaB) fructose-1,6-bisphosphate aldolase [5] (data from MRSA252) SACOL1329 (femC) glutamine synthetase [5] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [5] (data from MRSA252) SACOL0593 (fusA) elongation factor G [5] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [5] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [5] (data from MRSA252) SACOL1961 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [5] (data from MRSA252) SACOL1960 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [5] (data from MRSA252) SACOL2145 (glmS) glucosamine--fructose-6-phosphate aminotransferase [5] (data from MRSA252) SACOL1622 (glyS) glycyl-tRNA synthetase [5] (data from MRSA252) SACOL1554 (gnd) 6-phosphogluconate dehydrogenase [5] (data from MRSA252) SACOL2016 (groEL) chaperonin GroEL [5] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [5] (data from MRSA252) SACOL1288 (infB) translation initiation factor IF-2 [5] (data from MRSA252) SACOL2092 (murAA) UDP-N-acetylglucosamine 1-carboxyvinyltransferase [5] (data from MRSA252) SACOL2116 (murAB) UDP-N-acetylglucosamine 1-carboxyvinyltransferase [5] (data from MRSA252) SACOL1509 (ndk) nucleoside diphosphate kinase [5] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [5] (data from MRSA252) SACOL2128 (pdp) pyrimidine-nucleoside phosphorylase [5] (data from MRSA252) SACOL1746 (pfkA) 6-phosphofructokinase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL0966 (pgi) glucose-6-phosphate isomerase [5] (data from MRSA252) SACOL0841 (pgm) phosphoglyceromutase [5] (data from MRSA252) SACOL1091 (ptsH) phosphocarrier protein HPr [5] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [5] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [5] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [5] (data from MRSA252) SACOL2224 (rplF) 50S ribosomal protein L6 [5] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [5] (data from MRSA252) SACOL0583 (rplK) 50S ribosomal protein L11 [5] (data from MRSA252) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [5] (data from MRSA252) SACOL2212 (rplQ) 50S ribosomal protein L17 [5] (data from MRSA252) SACOL1702 (rplU) 50S ribosomal protein L21 [5] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [5] (data from MRSA252) SACOL0545 (rplY) 50S ribosomal protein L25/general stress protein Ctc [5] (data from MRSA252) SACOL2231 (rpmC) 50S ribosomal protein L29 [5] (data from MRSA252) SACOL2213 (rpoA) DNA-directed RNA polymerase subunit alpha [5] (data from MRSA252) SACOL0589 (rpoC) DNA-directed RNA polymerase subunit beta' [5] (data from MRSA252) SACOL1516 (rpsA) 30S ribosomal protein S1 [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [5] (data from MRSA252) SACOL1769 (rpsD) 30S ribosomal protein S4 [5] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [5] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [5] (data from MRSA252) SACOL2240 (rpsJ) 30S ribosomal protein S10 [5] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [5] (data from MRSA252) SACOL1262 (sucC) succinyl-CoA synthetase subunit beta [5] (data from MRSA252) SACOL1831 (tal) translaldolase [5] (data from MRSA252) SACOL1722 (tig) trigger factor [5] (data from MRSA252) SACOL1377 (tkt) transketolase [5] (data from MRSA252) SACOL1155 (trxA) thioredoxin [5] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [5] (data from MRSA252) SACOL2104 (upp) uracil phosphoribosyltransferase [5] (data from MRSA252) SACOL0564 pyridoxal biosynthesis lyase PdxS [5] (data from MRSA252) SACOL0617 hexulose-6-phosphate synthase [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL0742 hypothetical protein [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL1594 glycine dehydrogenase subunit 1 [5] (data from MRSA252) SACOL1670 hypothetical protein [5] (data from MRSA252) SACOL1759 universal stress protein [5] (data from MRSA252) SACOL2569 1-pyrroline-5-carboxylate dehydrogenase [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulators: CodY (repression) regulon, GltC (activation) regulon
CodY (TF) important in Amino acid metabolism; RegPrecise GltC (TF) important in Glutamate metabolism; RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟Protein stability[edit | edit source]
- half-life: 8.14 h [6]
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
PLoS One: 2009, 4(12);e8176
[PubMed:19997597] [WorldCat.org] [DOI] (I e) - ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
J Proteome Res: 2011, 10(4);1657-66
[PubMed:21323324] [WorldCat.org] [DOI] (I p) - ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
The Staphylococcus aureus proteome.
Int J Med Microbiol: 2014, 304(2);110-20
[PubMed:24439828] [WorldCat.org] [DOI] (I p) - ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
Sci Rep: 2016, 6;28172
[PubMed:27344979] [WorldCat.org] [DOI] (I e) - ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 5.40 5.41 5.42 5.43 5.44 5.45 5.46 5.47 5.48 5.49 5.50 5.51 5.52 5.53 5.54 5.55 5.56 5.57 5.58 5.59 5.60 5.61 5.62 5.63 5.64 5.65 5.66 5.67 5.68 5.69 5.70 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
J Proteome Res: 2011, 10(3);1139-50
[PubMed:21166474] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
Mol Cell Proteomics: 2012, 11(9);558-70
[PubMed:22556279] [WorldCat.org] [DOI] (I p)