※ Protein Information
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
Sequence Annotation From UniProt
 MOD_RES 1003 1003 O-(pantetheine 4'-phosphoryl)serine
Key Word From UniProt
 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
  IPR010071   AA_adenyl_domain.
  IPR009081   Acyl_carrier_prot-like.
  IPR025110   AMP-bd_C.
  IPR020845   AMP-binding_CS.
  IPR000873   AMP-dep_Synth/Lig.
  IPR001242   Condensatn.
  IPR006162   PPantetheine_attach_site.
  IPR001031   Thioesterase.
  PF00501   AMP-binding.
  PF13193   AMP-binding_C.
  PF00668   Condensation.
  PF00550   PP-binding.
  PF00975   Thioesterase.
  PS50075   ACP_DOMAIN.
  PS00455   AMP_BINDING.
  PS00012   PHOSPHOPANTETHEINE.