| Tag | Content |
|---|
| CPLM ID | CPLM-011633 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Surfactin synthase subunit 3 |
Protein Synonyms/Alias | |
Gene Name | srfAC |
Gene Synonyms/Alias | srfA3; BSU03510 |
Created Date | July 27, 2013 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 522 | SVVALYTKRSLELVI | acetylation | [1] | | 956 | VNKRLLPKPDQDQLA | acetylation | [1] |
|
Reference | [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG. Proteomics. 2013 May;13(10-11):1726-36. [ PMID: 23468065] |
Functional Description | Probably activates a leucine. |
Sequence Annotation | DOMAIN 973 1040 Acyl carrier.
REGION 1059 1271 Thioesterase.
ACT_SITE 1120 1120
ACT_SITE 1147 1147
ACT_SITE 1247 1247
MOD_RES 1003 1003 O-(pantetheine 4'-phosphoryl)serine |
Keyword | 3D-structure; Antibiotic biosynthesis; Complete proteome; Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Sporulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1275 AA |
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 |
Gene Ontology | 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. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |