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Protein

Surfactin synthase subunit 3

Gene

srfAC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably activates a leucine.

Cofactori

pantetheine 4'-phosphateNote: Binds 1 phosphopantetheine covalently.

Pathwayi: surfactin biosynthesis

This protein is involved in the pathway surfactin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway surfactin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei11201
Active sitei11471
Active sitei12471

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Antibiotic biosynthesis, Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU03510-MONOMER.
SABIO-RKQ08787.
UniPathwayiUPA00181.

Protein family/group databases

ESTHERibacsu-srfac. Thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Surfactin synthase subunit 3
Gene namesi
Name:srfAC
Synonyms:srfA3
Ordered Locus Names:BSU03510
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001931011 – 1275Surfactin synthase subunit 3Add BLAST1275

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1003O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiQ08787.
PRIDEiQ08787.

Interactioni

Protein-protein interaction databases

IntActiQ08787. 2 interactors.
MINTiMINT-8365036.
STRINGi224308.Bsubs1_010100001993.

Structurei

Secondary structure

11275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni1026 – 1028Combined sources3
Helixi1032 – 1041Combined sources10
Beta strandi1044 – 1046Combined sources3
Turni1047 – 1049Combined sources3
Beta strandi1050 – 1054Combined sources5
Beta strandi1058 – 1064Combined sources7
Helixi1071 – 1074Combined sources4
Helixi1075 – 1080Combined sources6
Beta strandi1084 – 1089Combined sources6
Helixi1097 – 1108Combined sources12
Beta strandi1114 – 1119Combined sources6
Helixi1121 – 1135Combined sources15
Beta strandi1140 – 1147Combined sources8
Helixi1166 – 1172Combined sources7
Turni1173 – 1175Combined sources3
Helixi1178 – 1180Combined sources3
Helixi1182 – 1201Combined sources20
Beta strandi1208 – 1216Combined sources9
Beta strandi1225 – 1228Combined sources4
Helixi1231 – 1233Combined sources3
Beta strandi1234 – 1236Combined sources3
Beta strandi1238 – 1242Combined sources5
Helixi1247 – 1249Combined sources3
Helixi1253 – 1267Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JMKX-ray1.71C/O1042-1271[»]
2VSQX-ray2.60A1016-1275[»]
ProteinModelPortaliQ08787.
SMRiQ08787.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini973 – 1040Acyl carrierPROSITE-ProRule annotationAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1059 – 1271ThioesteraseAdd BLAST213

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3319. LUCA.
HOGENOMiHOG000229993.
InParanoidiQ08787.
KOiK15656.
OMAiYLSPMQE.
PhylomeDBiQ08787.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQFSKDQVQ DMYYLSPMQE GMLFHAILNP GQSFYLEQIT MKVKGSLNIK
60 70 80 90 100
CLEESMNVIM DRYDVFRTVF IHEKVKRPVQ VVLKKRQFHI EEIDLTHLTG
110 120 130 140 150
SEQTAKINEY KEQDKIRGFD LTRDIPMRAA IFKKAEESFE WVWSYHHIIL
160 170 180 190 200
DGWCFGIVVQ DLFKVYNALR EQKPYSLPPV KPYKDYIKWL EKQDKQASLR
210 220 230 240 250
YWREYLEGFE GQTTFAEQRK KQKDGYEPKE LLFSLSEAET KAFTELAKSQ
260 270 280 290 300
HTTLSTALQA VWSVLISRYQ QSGDLAFGTV VSGRPAEIKG VEHMVGLFIN
310 320 330 340 350
VVPRRVKLSE GITFNGLLKR LQEQSLQSEP HQYVPLYDIQ SQADQPKLID
360 370 380 390 400
HIIVFENYPL QDAKNEESSE NGFDMVDVHV FEKSNYDLNL MASPGDEMLI
410 420 430 440 450
KLAYNENVFD EAFILRLKSQ LLTAIQQLIQ NPDQPVSTIN LVDDREREFL
460 470 480 490 500
LTGLNPPAQA HETKPLTYWF KEAVNANPDA PALTYSGQTL SYRELDEEAN
510 520 530 540 550
RIARRLQKHG AGKGSVVALY TKRSLELVIG ILGVLKAGAA YLPVDPKLPE
560 570 580 590 600
DRISYMLADS AAACLLTHQE MKEQAAELPY TGTTLFIDDQ TRFEEQASDP
610 620 630 640 650
ATAIDPNDPA YIMYTSGTTG KPKGNITTHA NIQGLVKHVD YMAFSDQDTF
660 670 680 690 700
LSVSNYAFDA FTFDFYASML NAARLIIADE HTLLDTERLT DLILQENVNV
710 720 730 740 750
MFATTALFNL LTDAGEDWMK GLRCILFGGE RASVPHVRKA LRIMGPGKLI
760 770 780 790 800
NCYGPTEGTV FATAHVVHDL PDSISSLPIG KPISNASVYI LNEQSQLQPF
810 820 830 840 850
GAVGELCISG MGVSKGYVNR ADLTKEKFIE NPFKPGETLY RTGDLARWLP
860 870 880 890 900
DGTIEYAGRI DDQVKIRGHR IELEEIEKQL QEYPGVKDAV VVADRHESGD
910 920 930 940 950
ASINAYLVNR TQLSAEDVKA HLKKQLPAYM VPQTFTFLDE LPLTTNGKVN
960 970 980 990 1000
KRLLPKPDQD QLAEEWIGPR NEMEETIAQI WSEVLGRKQI GIHDDFFALG
1010 1020 1030 1040 1050
GHSLKAMTAA SRIKKELGID LPVKLLFEAP TIAGISAYLK NGGSDGLQDV
1060 1070 1080 1090 1100
TIMNQDQEQI IFAFPPVLGY GLMYQNLSSR LPSYKLCAFD FIEEEDRLDR
1110 1120 1130 1140 1150
YADLIQKLQP EGPLTLFGYS AGCSLAFEAA KKLEEQGRIV QRIIMVDSYK
1160 1170 1180 1190 1200
KQGVSDLDGR TVESDVEALM NVNRDNEALN SEAVKHGLKQ KTHAFYSYYV
1210 1220 1230 1240 1250
NLISTGQVKA DIDLLTSGAD FDMPEWLASW EEATTGVYRV KRGFGTHAEM
1260 1270
LQGETLDRNA EILLEFLNTQ TVTVS
Length:1,275
Mass (Da):143,872
Last modified:June 16, 2009 - v2
Checksum:iC17C1685127BAF56
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26A → P in CAA49818 (PubMed:8355609).Curated1
Sequence conflicti26A → P in BAA08985 (PubMed:8969502).Curated1
Sequence conflicti33S → T in CAA49818 (PubMed:8355609).Curated1
Sequence conflicti33S → T in BAA08985 (PubMed:8969502).Curated1
Sequence conflicti1010 – 1015ASRIKK → VPHQQ in CAA49818 (PubMed:8355609).Curated6
Sequence conflicti1010 – 1015ASRIKK → VPHQQ in BAA08985 (PubMed:8969502).Curated6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70356 Genomic DNA. Translation: CAA49818.1.
D50453 Genomic DNA. Translation: BAA08985.1.
AL009126 Genomic DNA. Translation: CAB12145.2.
PIRiI40487.
RefSeqiNP_388233.2. NC_000964.3.
WP_003234570.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12145; CAB12145; BSU03510.
GeneIDi938308.
KEGGibsu:BSU03510.
PATRICi18972265. VBIBacSub10457_0361.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70356 Genomic DNA. Translation: CAA49818.1.
D50453 Genomic DNA. Translation: BAA08985.1.
AL009126 Genomic DNA. Translation: CAB12145.2.
PIRiI40487.
RefSeqiNP_388233.2. NC_000964.3.
WP_003234570.1. NZ_JNCM01000031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JMKX-ray1.71C/O1042-1271[»]
2VSQX-ray2.60A1016-1275[»]
ProteinModelPortaliQ08787.
SMRiQ08787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ08787. 2 interactors.
MINTiMINT-8365036.
STRINGi224308.Bsubs1_010100001993.

Protein family/group databases

ESTHERibacsu-srfac. Thioesterase.

Proteomic databases

PaxDbiQ08787.
PRIDEiQ08787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12145; CAB12145; BSU03510.
GeneIDi938308.
KEGGibsu:BSU03510.
PATRICi18972265. VBIBacSub10457_0361.

Phylogenomic databases

eggNOGiCOG3319. LUCA.
HOGENOMiHOG000229993.
InParanoidiQ08787.
KOiK15656.
OMAiYLSPMQE.
PhylomeDBiQ08787.

Enzyme and pathway databases

UniPathwayiUPA00181.
BioCyciBSUB:BSU03510-MONOMER.
SABIO-RKQ08787.

Miscellaneous databases

EvolutionaryTraceiQ08787.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRFAC_BACSU
AccessioniPrimary (citable) accession number: Q08787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: November 2, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The phosphoserine observed at Ser-1003 in PubMed:17218307 may result from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.