Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Surfactin synthase subunit 3 |
Protein Synonyms/Alias | |
Gene Name | srfAC |
Gene Synonyms/Alias | srfA3; OrderedLocusNames=BSU03510 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | 1003 | FFALGGHSLKAMTAA | S | HTP | [1],UniProt | |
Reference | [1]The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Macek B,Mijakovic I,Olsen JV,Gnad F,Kumar C,Jensen PR,Mann M Mol. Cell Proteomics 2007, Apr;6(4):697-707. [ PMID:17218307] |
Functional Description From UniProt | FUNCTION: Probably activates a leucine |
| MOD_RES 1003 1003 O-(pantetheine 4'-phosphoryl)serine |
| 3D-structure; Antibioticbiosynthesis; Completeproteome; Ligase; Phosphopantetheine; Phosphoprotein; Referenceproteome; Sporulation |
Protein Sequence | MSQFSKDQVQ DMYYLSPMQE GMLFHAILNP GQSFYLEQIT MKVKGSLNIK CLEESMNVIM 60 DRYDVFRTVF IHEKVKRPVQ VVLKKRQFHI EEIDLTHLTG SEQTAKINEY KEQDKIRGFD 120 LTRDIPMRAA IFKKAEESFE WVWSYHHIIL DGWCFGIVVQ DLFKVYNALR EQKPYSLPPV 180 KPYKDYIKWL EKQDKQASLR YWREYLEGFE GQTTFAEQRK KQKDGYEPKE LLFSLSEAET 240 KAFTELAKSQ HTTLSTALQA VWSVLISRYQ QSGDLAFGTV VSGRPAEIKG VEHMVGLFIN 300 VVPRRVKLSE GITFNGLLKR LQEQSLQSEP HQYVPLYDIQ SQADQPKLID HIIVFENYPL 360 QDAKNEESSE NGFDMVDVHV FEKSNYDLNL MASPGDEMLI KLAYNENVFD EAFILRLKSQ 420 LLTAIQQLIQ NPDQPVSTIN LVDDREREFL LTGLNPPAQA HETKPLTYWF KEAVNANPDA 480 PALTYSGQTL SYRELDEEAN RIARRLQKHG AGKGSVVALY TKRSLELVIG ILGVLKAGAA 540 YLPVDPKLPE DRISYMLADS AAACLLTHQE MKEQAAELPY TGTTLFIDDQ TRFEEQASDP 600 ATAIDPNDPA YIMYTSGTTG KPKGNITTHA NIQGLVKHVD YMAFSDQDTF LSVSNYAFDA 660 FTFDFYASML NAARLIIADE HTLLDTERLT DLILQENVNV MFATTALFNL LTDAGEDWMK 720 GLRCILFGGE RASVPHVRKA LRIMGPGKLI NCYGPTEGTV FATAHVVHDL PDSISSLPIG 780 KPISNASVYI LNEQSQLQPF GAVGELCISG MGVSKGYVNR ADLTKEKFIE NPFKPGETLY 840 RTGDLARWLP DGTIEYAGRI DDQVKIRGHR IELEEIEKQL QEYPGVKDAV VVADRHESGD 900 ASINAYLVNR TQLSAEDVKA HLKKQLPAYM VPQTFTFLDE LPLTTNGKVN KRLLPKPDQD 960 QLAEEWIGPR NEMEETIAQI WSEVLGRKQI GIHDDFFALG GHSLKAMTAA SRIKKELGID 1020 LPVKLLFEAP TIAGISAYLK NGGSDGLQDV TIMNQDQEQI IFAFPPVLGY GLMYQNLSSR 1080 LPSYKLCAFD FIEEEDRLDR YADLIQKLQP EGPLTLFGYS AGCSLAFEAA KKLEEQGRIV 1140 QRIIMVDSYK KQGVSDLDGR TVESDVEALM NVNRDNEALN SEAVKHGLKQ KTHAFYSYYV 1200 NLISTGQVKA DIDLLTSGAD FDMPEWLASW EEATTGVYRV KRGFGTHAEM LQGETLDRNA 1260 EILLEFLNTQ TVTVS 1275 |
| GO:0016788 F:hydrolase activity, acting on ester bonds IEA:InterPro GO:0016874 F:ligase activity IEA:UniProtKB-KW GO:0017000 P:antibiotic biosynthetic process IEA:UniProtKB-KW GO:0030435 P:sporulation resulting in formation of a cellular spore IEA:UniProtKB-KW |
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