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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01176
- pan locus tag?: SAUPAN003491000
- symbol: gmk
- pan gene symbol?: gmk
- synonym:
- product: guanylate kinase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
⊟Accession numbers[edit | edit source]
- Gene ID: 3920927 NCBI
- RefSeq: YP_499715 NCBI
- BioCyc: G1I0R-1102 BioCyc
- MicrobesOnline: 1289629 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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601ATGGATAATGAAAAAGGATTGTTAATCGTTTTATCAGGACCATCTGGAGTAGGTAAAGGT
ACTGTTAGAAAACGAATATTTGAAGATCCAAGTACATCATATAAGTATTCTATTTCAATG
ACAACACGTCAAATGCGTGAAGGTGAAGTTGATGGCGTAGATTACTTTTTTAAAACTAGG
GATGCGTTTGAAGCTTTAATCAAAGATGACCAATTTATAGAATATGCTGAATATGTAGGC
AACTATTATGGTACACCAGTTCAATATGTTAAAGATACAATGGACGAAGGTCATGATGTA
TTTTTAGAAATTGAAGTAGAAGGTGCAAAGCAAGTTAGAAAGAAATTTCCAGATGCGCTA
TTTATTTTCTTAGCACCTCCAAGTTTAGAACACTTGAGAGAGCGATTAGTAGGTAGAGGA
ACAGAATCTGATGAGAAAATACAAAGTCGTATTAACGAAGCGCGTAAAGAAGTTGAAATG
ATGAATTTATACGATTACGTTGTAGTTAATGATGAAGTAGAACTTGCGAAGAATAGAATT
CAATGTATTGTAGAAGCTGAGCACTTAAAAAGAGAGCGCGTAGAAGCTAAGTATAGAAAA
ATGATTTTGGAGGCTAAAAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01176
- symbol: Gmk
- description: guanylate kinase
- length: 207
- theoretical pI: 5.10267
- theoretical MW: 24037.2
- GRAVY: -0.579227
⊟Function[edit | edit source]
- reaction: EC 2.7.4.8? ExPASyGuanylate kinase ATP + GMP = ADP + GDP
- TIGRFAM: Purines, pyrimidines, nucleosides, and nucleotides Nucleotide and nucleoside interconversions guanylate kinase (TIGR03263; EC 2.7.4.8; HMM-score: 238.9)and 5 moreCentral intermediary metabolism Phosphorus compounds phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN (TIGR02322; HMM-score: 47.8)Biosynthesis of cofactors, prosthetic groups, and carriers Pantothenate and coenzyme A dephospho-CoA kinase (TIGR00152; EC 2.7.1.24; HMM-score: 19)putative cytidylate kinase (TIGR02173; EC 2.7.4.14; HMM-score: 14.1)Purines, pyrimidines, nucleosides, and nucleotides Nucleotide and nucleoside interconversions adenylate kinase (TIGR01351; EC 2.7.4.-; HMM-score: 13.5)phosphonate C-P lyase system protein PhnL (TIGR02324; HMM-score: 12.4)
- TheSEED :
- Guanylate kinase (EC 2.7.4.8)
- PFAM: P-loop_NTPase (CL0023) Guanylate_kin; Guanylate kinase (PF00625; HMM-score: 172.1)and 9 moreAAA_18; AAA domain (PF13238; HMM-score: 19.7)MMR_HSR1; 50S ribosome-binding GTPase (PF01926; HMM-score: 14.3)AAA_16; AAA ATPase domain (PF13191; HMM-score: 14.3)AAA_17; AAA domain (PF13207; HMM-score: 14.1)AAA_22; AAA domain (PF13401; HMM-score: 14.1)AAA_33; AAA domain (PF13671; HMM-score: 13.8)ABC_tran; ABC transporter (PF00005; HMM-score: 13.6)no clan defined YtxH; YtxH-like protein (PF12732; HMM-score: 13.2)P-loop_NTPase (CL0023) RsgA_GTPase; RsgA GTPase (PF03193; HMM-score: 11.9)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.97
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0.01
- Extracellular Score: 0.02
- 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): 0.006276
- TAT(Tat/SPI): 0.000768
- LIPO(Sec/SPII): 0.002138
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MDNEKGLLIVLSGPSGVGKGTVRKRIFEDPSTSYKYSISMTTRQMREGEVDGVDYFFKTRDAFEALIKDDQFIEYAEYVGNYYGTPVQYVKDTMDEGHDVFLEIEVEGAKQVRKKFPDALFIFLAPPSLEHLRERLVGRGTESDEKIQSRINEARKEVEMMNLYDYVVVNDEVELAKNRIQCIVEAEHLKRERVEAKYRKMILEAKK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [2] [3]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_00799 (eno) phosphopyruvate hydratase [4] (data from MRSA252) SAOUHSC_02254 (groEL) chaperonin GroEL [4] (data from MRSA252) SAOUHSC_01159 (ileS) isoleucyl-tRNA synthetase [4] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [4] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [4] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [4] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [4] (data from MRSA252) SAOUHSC_02484 (rplQ) 50S ribosomal protein L17 [4] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [4] (data from MRSA252) SAOUHSC_01493 (rpsA) 30S ribosomal protein S1 [4] (data from MRSA252) SAOUHSC_00348 (rpsF) 30S ribosomal protein S6 [4] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [4] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [4] (data from MRSA252) SAOUHSC_01216 (sucC) succinyl-CoA synthetase subunit beta [4] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [4] (data from MRSA252) SAOUHSC_00336 acetyl-CoA acyltransferase [4] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [4] (data from MRSA252) SAOUHSC_00679 hypothetical protein [4] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [4] (data from MRSA252) SAOUHSC_00798 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [4] (data from MRSA252) SAOUHSC_00937 oligoendopeptidase F [4] (data from MRSA252) SAOUHSC_00951 hypothetical protein [4] (data from MRSA252) SAOUHSC_01007 bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase [4] (data from MRSA252) SAOUHSC_01028 phosphocarrier protein HPr [4] (data from MRSA252) SAOUHSC_01100 thioredoxin [4] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [4] (data from MRSA252) SAOUHSC_01199 3-oxoacyl-(acyl-carrier-protein) reductase [4] (data from MRSA252) SAOUHSC_01287 glutamine synthetase [4] (data from MRSA252) SAOUHSC_01666 glycyl-tRNA synthetase [4] (data from MRSA252) SAOUHSC_01719 hypothetical protein [4] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [4] (data from MRSA252) SAOUHSC_02366 fructose-bisphosphate aldolase [4] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [5] Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: no data available
⊟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]
- ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
BMC Genomics: 2009, 10;291
[PubMed:19570206] [WorldCat.org] [DOI] (I e) - ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 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) - ↑ 5.0 5.1 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)