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Protein

4'-phosphopantetheinyl transferase sfp

Gene

sfp

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

Functioni

Activates the seven peptidyl carrier protein (PCP) domains of surfactin synthase SRF1/2/3 by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for cells of B.subtilis to become producers of the lipopeptide antibiotics surfactin and plipastatin B1.1 Publication

Catalytic activityi

CoA + apo-[peptidyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein].

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi107Magnesium1
Metal bindingi109Magnesium1
Metal bindingi151Magnesium1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13919.

Names & Taxonomyi

Protein namesi
Recommended name:
4'-phosphopantetheinyl transferase sfp (EC:2.7.8.-)
Alternative name(s):
Surfactin synthase-activating enzyme
Gene namesi
Name:sfp
Synonyms:lpa-8
Ordered Locus Names:BSU03570
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105G → A: Almost no activity. 1 Publication1
Mutagenesisi105G → D: Loss of activity. 1 Publication1
Mutagenesisi107D → A: Loss of activity. 1 Publication1
Mutagenesisi107D → E: 3000-fold reduction in activity, but no change in substrate affinity. 1 Publication1
Mutagenesisi147W → A: 24-fold reduction in activity, but no change in substrate affinity. 1 Publication1
Mutagenesisi147W → F: 5-fold reduction in activity, but no change in substrate affinity. 1 Publication1
Mutagenesisi151E → A: Loss of activity. 1 Publication1
Mutagenesisi155K → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002060771 – 2244'-phosphopantetheinyl transferase sfpAdd BLAST224

Proteomic databases

PaxDbiP39135.

Interactioni

Subunit structurei

Monomer in solution.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002028.

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi14 – 21Combined sources8
Helixi26 – 34Combined sources9
Helixi38 – 58Combined sources21
Helixi63 – 65Combined sources3
Beta strandi85 – 91Combined sources7
Beta strandi94 – 102Combined sources9
Beta strandi105 – 110Combined sources6
Helixi116 – 119Combined sources4
Beta strandi120 – 123Combined sources4
Helixi125 – 133Combined sources9
Helixi136 – 157Combined sources22
Helixi160 – 162Combined sources3
Helixi165 – 167Combined sources3
Beta strandi169 – 172Combined sources4
Helixi174 – 176Combined sources3
Beta strandi178 – 181Combined sources4
Beta strandi190 – 194Combined sources5
Beta strandi200 – 209Combined sources10
Helixi220 – 224Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QR0X-ray1.90A1-224[»]
2GE0model-A1-224[»]
2GE1model-A1-224[»]
4MRTX-ray2.00A1-224[»]
ProteinModelPortaliP39135.
SMRiP39135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39135.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 189Peptidyl carrier protein bindingSequence analysisAdd BLAST32

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105W8Z. Bacteria.
COG2091. LUCA.
InParanoidiP39135.

Family and domain databases

Gene3Di3.90.470.20. 2 hits.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR004568. Ppantetheine-prot_Trfase_dom.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
[Graphical view]
SUPFAMiSSF56214. SSF56214. 2 hits.
TIGRFAMsiTIGR00556. pantethn_trn. 1 hit.

Sequencei

Sequence statusi: Complete.

P39135-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIYGIYMDR PLSQEENERF MSFISPEKRE KCRRFYHKED AHRTLLGDVL
60 70 80 90 100
VRSVISRQYQ LDKSDIRFST QEYGKPCIPD LPDAHFNISH SGRWVICAFD
110 120 130 140 150
SQPIGIDIEK TKPISLEIAK RFFSKTEYSD LLAKDKDEQT DYFYHLWSMK
160 170 180 190 200
ESFIKQEGKG LSLPLDSFSV RLHQDGQVSI ELPDSHSPCY IKTYEVDPGY
210 220
KMAVCAAHPD FPEDITMVSY EELL
Length:224
Mass (Da):26,168
Last modified:June 16, 2009 - v2
Checksum:i0FEFB5D9D3534C68
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti118 – 119IA → MP in CAA46561 (PubMed:8355609).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti22S → T in strain: oKB105. 1
Natural varianti97C → G in strain: oKB105. 1
Natural varianti157 – 224EGKGL…YEELL → GRQRLIASA in strain 168 and its derivatives, non surfactin-producing strains. Add BLAST68

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63158 Genomic DNA. Translation: CAA44858.1.
X65610 Genomic DNA. Translation: CAA46561.1.
L17438 Unassigned DNA. Translation: AAC36829.1.
X70356 Genomic DNA. No translation available.
D50562 Genomic DNA. Translation: BAA09125.1.
AL009126 Genomic DNA. Translation: CAB12151.2.
PIRiS20463.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63158 Genomic DNA. Translation: CAA44858.1.
X65610 Genomic DNA. Translation: CAA46561.1.
L17438 Unassigned DNA. Translation: AAC36829.1.
X70356 Genomic DNA. No translation available.
D50562 Genomic DNA. Translation: BAA09125.1.
AL009126 Genomic DNA. Translation: CAB12151.2.
PIRiS20463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QR0X-ray1.90A1-224[»]
2GE0model-A1-224[»]
2GE1model-A1-224[»]
4MRTX-ray2.00A1-224[»]
ProteinModelPortaliP39135.
SMRiP39135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002028.

Proteomic databases

PaxDbiP39135.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105W8Z. Bacteria.
COG2091. LUCA.
InParanoidiP39135.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13919.

Miscellaneous databases

EvolutionaryTraceiP39135.

Family and domain databases

Gene3Di3.90.470.20. 2 hits.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR004568. Ppantetheine-prot_Trfase_dom.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
[Graphical view]
SUPFAMiSSF56214. SSF56214. 2 hits.
TIGRFAMsiTIGR00556. pantethn_trn. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSFP_BACSU
AccessioniPrimary (citable) accession number: P39135
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: November 2, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Strain 168 and its derivatives encode a truncated, inactive version of this protein. The sequence shown here corresponds to that of strain ATCC 21332 which is active.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.