P39135 (SFP_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4'-phosphopantetheinyl transferase sfp
EC=2.7.8.-

Alternative name(s):
Surfactin synthase-activating enzyme

Gene names

Name:	sfp
Synonyms:	lpa-8
Ordered Locus Names:	BSU03570

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7
Catalytic activity	CoA + apo-[peptidyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein].
Cofactor	Magnesium.
Subunit structure	Monomer in solution.
Sequence similarities	Belongs to the P-Pant transferase superfamily. Gsp/sfp/hetI/acpT family.
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.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro macromolecule biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	holo-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 224

224

4'-phosphopantetheinyl transferase sfp

PRO_0000206077

Regions

Region

158 – 189

32

Peptidyl carrier protein binding Potential

Sites

Metal binding

107

1

Magnesium

Metal binding

109

1

Magnesium

Metal binding

151

1

Magnesium

Natural variations

Natural variant

22

1

S → T in strain oKB105.

Natural variant

97

1

C → G in strain oKB105.

Natural variant

157 – 224

68

EGKGL…YEELL → GRQRLIASA in strain 168 and its derivatives, non surfactin-producing strains.

Experimental info

Mutagenesis

105

1

G → A: Almost no activity. Ref.8

Mutagenesis

105

1

G → D: Loss of activity. Ref.8

Mutagenesis

107

1

D → A: Loss of activity. Ref.8

Mutagenesis

107

1

D → E: 3000-fold reduction in activity, but no change in substrate affinity. Ref.8

Mutagenesis

147

1

W → A: 24-fold reduction in activity, but no change in substrate affinity. Ref.8

Mutagenesis

147

1

W → F: 5-fold reduction in activity, but no change in substrate affinity. Ref.8

Mutagenesis

151

1

E → A: Loss of activity. Ref.8

Mutagenesis

155

1

K → A: Loss of activity. Ref.8

Sequence conflict

118 – 119

2

IA → MP in CAA46561. Ref.3

Secondary structure

1

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224

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

14 – 21

8

Helix

26 – 34

9

Helix

38 – 58

21

Helix

63 – 65

3

Beta strand

85 – 91

7

Beta strand

94 – 102

9

Beta strand

105 – 110

6

Helix

116 – 119

4

Beta strand

120 – 123

4

Helix

125 – 133

9

Helix

136 – 157

22

Beta strand

169 – 172

4

Helix

174 – 176

3

Beta strand

177 – 181

5

Beta strand

190 – 194

5

Beta strand

200 – 209

10

Sequences

	Sequence		Length	Mass (Da)
	P39135 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 0FEFB5D9D3534C68	FASTA	224	26,168
	10 20 30 40 50 60 MKIYGIYMDR PLSQEENERF MSFISPEKRE KCRRFYHKED AHRTLLGDVL VRSVISRQYQ 70 80 90 100 110 120 LDKSDIRFST QEYGKPCIPD LPDAHFNISH SGRWVICAFD SQPIGIDIEK TKPISLEIAK 130 140 150 160 170 180 RFFSKTEYSD LLAKDKDEQT DYFYHLWSMK ESFIKQEGKG LSLPLDSFSV RLHQDGQVSI 190 200 210 220 ELPDSHSPCY IKTYEVDPGY KMAVCAAHPD FPEDITMVSY EELL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1557038] [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: 8407792] [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: 8355609] [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: 8639027] [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: 9384377] [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: 19383706] [Abstract] Cited for: SEQUENCE REVISION.
[7]	"A new enzyme superfamily -- the phosphopantetheinyl transferases." Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M., Marahiel M.A., Reid R., Khosla C., Walsh C.T. Chem. Biol. 3:923-936(1996) [PubMed: 8939709] [Abstract] 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: 9484229] [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: 10581256] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

S20463.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QR0	X-ray	1.90	A	1-224	[»]
2GE0	model	-	A	1-224	[»]
2GE1	model	-	A	1-224	[»]

ProteinModelPortal

P39135.

SMR

P39135. Positions 1-224.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

NMPDR

fig|224308.1.peg.358.

Organism-specific databases

GenoList

BSU03570. [Micado]

Phylogenomic databases

HOGENOM

HBG343452.

PhylomeDB

P39135.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13919.

Family and domain databases

InterPro

IPR008278. 4-PPantetheinyl_Trfase.
IPR004568. PPantethiene-prot_Trfase.
[Graphical view]

Gene3D

G3DSA:3.90.470.20. G3DSA:3.90.470.20. 1 hit.

Pfam

PF01648. ACPS. 1 hit.
[Graphical view]

SUPFAM

SSF56214. 4-PPT_transf. 2 hits.

TIGRFAMs

TIGR00556. Pantethn_trn. 1 hit.

ProtoNet

Search...

Entry information

Entry name

SFP_BACSU

Accession

Primary (citable) accession number: P39135

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	June 16, 2009
Last modified:	December 14, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program