Jump to navigation
Jump to search
NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0987 [new locus tag: SACOL_RS05050 ]
- pan locus tag?: SAUPAN003127000
- symbol: fabH
- pan gene symbol?: fabH
- synonym:
- product: 3-oxoacyl-ACP synthase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0987 [new locus tag: SACOL_RS05050 ]
- symbol: fabH
- product: 3-oxoacyl-ACP synthase
- replicon: chromosome
- strand: +
- coordinates: 994756..995697
- length: 942
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237317 NCBI
- RefSeq: YP_185855 NCBI
- BioCyc: see SACOL_RS05050
- MicrobesOnline: 912456 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
- 1
61
121
181
241
301
361
421
481
541
601
661
721
781
841
901ATGAACGTGGGTATTAAAGGTTTTGGTGCATATGCGCCAGAAAAGATTATTGACAATGCC
TATTTTGAGCAATTTTTAGATACATCTGATGAATGGATTTCTAAGATGACTGGAATTAAA
GAAAGACATTGGGCAGATGATGATCAAGATACTTCAGATTTAGCATATGAAGCAAGTTTA
AAAGCAATCGCTGACGCTGGTATTCAGCCCGAAGATATAGATATGATAATTGTTGCCACA
GCAACTGGAGATATGCCATTTCCAACTGTCGCAAATATGTTGCAAGAACGTTTAGGGACG
GGCAAAGTTGCCTCTATGGATCAACTTGCAGCATGTTCTGGATTTATGTATTCAATGATT
ACAGCTAAACAATATGTTCAATCTGGAGATTATCATAACATTTTAGTTGTCGGTGCAGAT
AAATTATCTAAAATAACAGATTTAACTGACCGTTCTACTGCAGTTCTATTTGGAGATGGT
GCAGGTGCGGTTATCATCGGTGAAGTTTCAGATGGCAGAGGTATTATAAGTTATGAAATG
GGTTCTGATGGCACAGGTGGTAAACATTTATATTTAGATAAAGATACTGGTAAACTGAAA
ATGAATGGTCGAGAAGTATTTAAATTTGCTGTTAGAATTATGGGTGATGCATCAACACGT
GTAGTTGAAAAAGCGAATTTAACATCAGATGATATAGATTTATTTATTCCTCATCAAGCT
AATATTAGAATTATGGAATCAGCTAGAGAACGCTTAGGTATTTCAAAAGACAAAATGAGT
GTTTCTGTAAATAAATATGGAAATACTTCAGCTGCGTCAATACCTTTAAGTATCGATCAA
GAATTAAAAAATGGTAAAATCAAAGATGATGATACAATTGTTCTTGTCGGATTCGGTGGC
GGCCTAACTTGGGGCGCAATGACAATAAAATGGGGAAAATAG60
120
180
240
300
360
420
480
540
600
660
720
780
840
900
942
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0987 [new locus tag: SACOL_RS05050 ]
- symbol: FabH
- description: 3-oxoacyl-ACP synthase
- length: 313
- theoretical pI: 4.63572
- theoretical MW: 33879.2
- GRAVY: -0.176997
⊟Function[edit | edit source]
- reaction: EC 2.3.1.41? ExPASyBeta-ketoacyl-[acyl-carrier-protein] synthase I Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]EC 2.3.1.180? ExPASyBeta-ketoacyl-[acyl-carrier-protein] synthase III Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2
- TIGRFAM: Fatty acid and phospholipid metabolism Biosynthesis 3-oxoacyl-[acyl-carrier-protein] synthase III (TIGR00747; EC 2.3.1.180; HMM-score: 409.2)and 5 moreFatty acid and phospholipid metabolism Biosynthesis putative hydroxymethylglutaryl-CoA synthase (TIGR00748; EC 2.3.3.10; HMM-score: 63.8)hydroxymethylglutaryl-CoA synthase (TIGR01835; EC 2.3.3.10; HMM-score: 31.5)Fatty acid and phospholipid metabolism Other acetyl-CoA C-acyltransferase (TIGR01930; EC 2.3.1.16; HMM-score: 28.9)hydroxymethylglutaryl-CoA synthase (TIGR01833; EC 2.3.3.10; HMM-score: 17.9)Cellular processes Sporulation and germination stage V sporulation protein AD (TIGR02845; HMM-score: 16.5)
- TheSEED :
- 3-oxoacyl-[acyl-carrier-protein] synthase, KASIII (EC 2.3.1.180)
- PFAM: Thiolase (CL0046) ACP_syn_III_C; 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal (PF08541; HMM-score: 128.9)and 8 moreACP_syn_III; 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III (PF08545; HMM-score: 98)Thiolase_N; Thiolase, N-terminal domain (PF00108; HMM-score: 39.5)Chal_sti_synt_N; Chalcone and stilbene synthases, N-terminal domain (PF00195; HMM-score: 24)SpoVAD; Stage V sporulation protein AD (SpoVAD) (PF07451; HMM-score: 20.9)Chal_sti_synt_C; Chalcone and stilbene synthases, C-terminal domain (PF02797; HMM-score: 19.5)HMG_CoA_synt_N; Hydroxymethylglutaryl-coenzyme A synthase N terminal (PF01154; HMM-score: 18.8)FAE1_CUT1_RppA; FAE1/Type III polyketide synthase-like protein (PF08392; HMM-score: 17.3)Thiolase_C; Thiolase, C-terminal domain (PF02803; HMM-score: 15.9)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.67
- Cytoplasmic Membrane Score: 0.01
- Cellwall Score: 0.15
- Extracellular Score: 0.17
- 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): 0.002447
- TAT(Tat/SPI): 0.000185
- LIPO(Sec/SPII): 0.000296
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASLKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDGAGAVIIGEVSDGRGIISYEMGSDGTGGKHLYLDKDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKIKDDDTIVLVGFGGGLTWGAMTIKWGK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 605 [4]
- interaction partners:
SACOL1253 (ffh) signal recognition particle protein [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) SACOL1727 (infC) translation initiation factor IF-3 [5] (data from MRSA252) SACOL1091 (ptsH) phosphocarrier protein HPr [5] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [5] (data from MRSA252) SACOL2238 (rplD) 50S ribosomal protein L4 [5] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [5] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [5] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [5] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [5] (data from MRSA252) SACOL2233 (rpsC) 30S ribosomal protein S3 [5] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [5] (data from MRSA252) SACOL0437 (rpsF) 30S ribosomal protein S6 [5] (data from MRSA252) SACOL0592 (rpsG) 30S ribosomal protein S7 [5] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [5] (data from MRSA252) SACOL0591 (rpsL) 30S ribosomal protein S12 [5] (data from MRSA252) SACOL0816 (secA) preprotein translocase subunit SecA [5] (data from MRSA252) SACOL2104 (upp) uracil phosphoribosyltransferase [5] (data from MRSA252) SACOL0455 hypothetical protein [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL2173 alkaline shock protein 23 [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: FapR* (repression) regulon
FapR* (TF) important in Fatty acid biosynthesis; RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: 24.51 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 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)