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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Magnesium
Metal bindingi109 – 1091Magnesium
Metal bindingi151 – 1511Magnesium

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051G → A: Almost no activity. 1 Publication
Mutagenesisi105 – 1051G → D: Loss of activity. 1 Publication
Mutagenesisi107 – 1071D → A: Loss of activity. 1 Publication
Mutagenesisi107 – 1071D → E: 3000-fold reduction in activity, but no change in substrate affinity. 1 Publication
Mutagenesisi147 – 1471W → A: 24-fold reduction in activity, but no change in substrate affinity. 1 Publication
Mutagenesisi147 – 1471W → F: 5-fold reduction in activity, but no change in substrate affinity. 1 Publication
Mutagenesisi151 – 1511E → A: Loss of activity. 1 Publication
Mutagenesisi155 – 1551K → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2242244'-phosphopantetheinyl transferase sfpPRO_0000206077Add
BLAST

Proteomic databases

PaxDbiP39135.

Interactioni

Subunit structurei

Monomer in solution.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002028.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi14 – 218Combined sources
Helixi26 – 349Combined sources
Helixi38 – 5821Combined sources
Helixi63 – 653Combined sources
Beta strandi85 – 917Combined sources
Beta strandi94 – 1029Combined sources
Beta strandi105 – 1106Combined sources
Helixi116 – 1194Combined sources
Beta strandi120 – 1234Combined sources
Helixi125 – 1339Combined sources
Helixi136 – 15722Combined sources
Helixi160 – 1623Combined sources
Helixi165 – 1673Combined sources
Beta strandi169 – 1724Combined sources
Helixi174 – 1763Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi200 – 20910Combined sources
Helixi220 – 2245Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP39135.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 18932Peptidyl carrier protein bindingSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1192IA → MP in CAA46561 (PubMed:8355609).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221S → T in strain: oKB105.
Natural varianti97 – 971C → G in strain: oKB105.
Natural varianti157 – 22468EGKGL…YEELL → GRQRLIASA in strain 168 and its derivatives, non surfactin-producing strains.
Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1QR0X-ray1.90A1-224[»]
2GE0model-A1-224[»]
2GE1model-A1-224[»]
4MRTX-ray2.00A1-224[»]
ProteinModelPortaliP39135.
SMRiP39135. Positions 1-224.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of sfp: a gene that functions in the production of the lipopeptide biosurfactant, surfactin, in Bacillus subtilis."
    Nakano M.M., Corbell N., Besson J., Zuber P.
    Mol. Gen. Genet. 232:313-321(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14.
    Strain: 168 and oKB105.
  2. "Isolation and characterization of Bacillus subtilis genes involved in siderophore biosynthesis: relationship between B. subtilis sfpo and Escherichia coli entD genes."
    Grossman T.H., Tuckman M., Ellestad S., Osburne M.S.
    J. Bacteriol. 175:6203-6211(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis."
    Cosmina P., Rodriguez F., de Ferra F., Grandi G., Perego M., Venema G., van Sinderen D.
    Mol. Microbiol. 8:821-831(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH624 and ATCC 21332 / IAM 1213.
  4. "Isolation of a gene essential for biosynthesis of the lipopeptide antibiotics plipastatin B1 and surfactin in Bacillus subtilis YB8."
    Tsuge K., Ano T., Shoda M.
    Arch. Microbiol. 165:243-251(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: YB8.
  5. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  6. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  7. Cited for: FUNCTION.
  8. "Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases."
    Quadri L.E.N., Weinreb P.H., Lei M., Nakano M.M., Zuber P., Walsh C.T.
    Biochemistry 37:1585-1595(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF GLY-105; ASP-107; TRP-147; GLU-151 AND LYS-155.
  9. "Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily."
    Reuter K., Mofid M.R., Marahiel M.A., Ficner R.
    EMBO J. 18:6823-6831(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

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: June 8, 2016
This is version 113 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.