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4'-phosphopantetheinyl transferase Sfp (EC 2.7.8.7) (Surfactin synthase-activating enzyme)

 SFP_BACSU               Reviewed;         224 AA.
P39135;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
23-MAY-2018, entry version 120.
RecName: Full=4'-phosphopantetheinyl transferase Sfp;
EC=2.7.8.7 {ECO:0000269|PubMed:11451672};
AltName: Full=Surfactin synthase-activating enzyme;
Name=sfp; Synonyms=lpa-8; OrderedLocusNames=BSU03570;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-14.
STRAIN=168, and oKB105;
PubMed=1557038;
Nakano M.M., Corbell N., Besson J., Zuber P.;
"Isolation and characterization of sfp: a gene that functions in the
production of the lipopeptide biosurfactant, surfactin, in Bacillus
subtilis.";
Mol. Gen. Genet. 232:313-321(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8407792; DOI=10.1128/jb.175.19.6203-6211.1993;
Grossman T.H., Tuckman M., Ellestad S., Osburne M.S.;
"Isolation and characterization of Bacillus subtilis genes involved in
siderophore biosynthesis: relationship between B. subtilis sfpo and
Escherichia coli entD genes.";
J. Bacteriol. 175:6203-6211(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH624, and ATCC 21332 / IAM 1213;
PubMed=8355609; DOI=10.1111/j.1365-2958.1993.tb01629.x;
Cosmina P., Rodriguez F., de Ferra F., Grandi G., Perego M.,
Venema G., van Sinderen D.;
"Sequence and analysis of the genetic locus responsible for surfactin
synthesis in Bacillus subtilis.";
Mol. Microbiol. 8:821-831(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=YB8;
PubMed=8639027; DOI=10.1007/s002030050322;
Tsuge K., Ano T., Shoda M.;
"Isolation of a gene essential for biosynthesis of the lipopeptide
antibiotics plipastatin B1 and surfactin in Bacillus subtilis YB8.";
Arch. Microbiol. 165:243-251(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[6]
SEQUENCE REVISION.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[7]
FUNCTION.
PubMed=8939709; DOI=10.1016/S1074-5521(96)90181-7;
Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M.,
Marahiel M.A., Reid R., Khosla C., Walsh C.T.;
"A new enzyme superfamily -- the phosphopantetheinyl transferases.";
Chem. Biol. 3:923-936(1996).
[8]
CHARACTERIZATION, AND MUTAGENESIS OF GLY-105; ASP-107; TRP-147;
GLU-151 AND LYS-155.
PubMed=9484229; DOI=10.1021/bi9719861;
Quadri L.E.N., Weinreb P.H., Lei M., Nakano M.M., Zuber P.,
Walsh C.T.;
"Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl
transferase for peptidyl carrier protein domains in peptide
synthetases.";
Biochemistry 37:1585-1595(1998).
[9]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11451672; DOI=10.1016/S1074-5521(01)00047-3;
Sanchez C., Du L., Edwards D.J., Toney M.D., Shen B.;
"Cloning and characterization of a phosphopantetheinyl transferase
from Streptomyces verticillus ATCC15003, the producer of the hybrid
peptide-polyketide antitumor drug bleomycin.";
Chem. Biol. 8:725-738(2001).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=10581256; DOI=10.1093/emboj/18.23.6823;
Reuter K., Mofid M.R., Marahiel M.A., Ficner R.;
"Crystal structure of the surfactin synthetase-activating enzyme sfp:
a prototype of the 4'-phosphopantetheinyl transferase superfamily.";
EMBO J. 18:6823-6831(1999).
-!- 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.
{ECO:0000269|PubMed:8939709}.
-!- CATALYTIC ACTIVITY: CoA-(4'-phosphopantetheine) + apo-[acyl-
carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-
carrier-protein]. {ECO:0000269|PubMed:11451672}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.7 uM for Streptomyces mobaraensis apo-PCP BlmI
{ECO:0000269|PubMed:9484229};
KM=11 uM for Streptomyces glaucescens apo-ACP TcmM
{ECO:0000269|PubMed:9484229};
Note=kcat is 7.2 min(-1) with S.mobaraensis apo-PCP BlmI as
substrate and 0.89 min(-1) with S.glaucescens apo-ACP TcmM as
substrate. {ECO:0000269|PubMed:9484229};
-!- SUBUNIT: Monomer in solution.
-!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
-!- 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.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X63158; CAA44858.1; -; Genomic_DNA.
EMBL; X65610; CAA46561.1; -; Genomic_DNA.
EMBL; L17438; AAC36829.1; -; Unassigned_DNA.
EMBL; X70356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D50562; BAA09125.1; -; Genomic_DNA.
EMBL; AL009126; CAB12151.2; -; Genomic_DNA.
PIR; S20463; S20463.
PDB; 1QR0; X-ray; 1.90 A; A=1-224.
PDB; 2GE0; Model; -; A=1-224.
PDB; 2GE1; Model; -; A=1-224.
PDB; 4MRT; X-ray; 2.00 A; A=1-224.
PDBsum; 1QR0; -.
PDBsum; 2GE0; -.
PDBsum; 2GE1; -.
PDBsum; 4MRT; -.
ProteinModelPortal; P39135; -.
SMR; P39135; -.
STRING; 224308.Bsubs1_010100002028; -.
DrugBank; DB01992; Coenzyme A.
PaxDb; P39135; -.
PRIDE; P39135; -.
eggNOG; ENOG4105W8Z; Bacteria.
eggNOG; COG2091; LUCA.
InParanoid; P39135; -.
BioCyc; MetaCyc:MONOMER-13919; -.
EvolutionaryTrace; P39135; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
GO; GO:1900192; P:positive regulation of single-species biofilm formation; IMP:CACAO.
Gene3D; 3.90.470.20; -; 3.
InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
Pfam; PF01648; ACPS; 1.
SUPFAM; SSF56214; SSF56214; 2.
TIGRFAMs; TIGR00556; pantethn_trn; 1.
1: Evidence at protein level;
3D-structure; Antibiotic biosynthesis; Complete proteome;
Direct protein sequencing; Magnesium; Metal-binding;
Reference proteome; Transferase.
CHAIN 1 224 4'-phosphopantetheinyl transferase Sfp.
/FTId=PRO_0000206077.
REGION 158 189 Peptidyl carrier protein binding.
{ECO:0000255}.
METAL 107 107 Magnesium.
METAL 109 109 Magnesium.
METAL 151 151 Magnesium.
VARIANT 22 22 S -> T (in strain: oKB105).
VARIANT 97 97 C -> G (in strain: oKB105).
VARIANT 157 224 EGKGLSLPLDSFSVRLHQDGQVSIELPDSHSPCYIKTYEVD
PGYKMAVCAAHPDFPEDITMVSYEELL -> GRQRLIASA
(in strain 168 and its derivatives, non
surfactin-producing strains).
MUTAGEN 105 105 G->A: Almost no activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 105 105 G->D: Loss of activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 107 107 D->A: Loss of activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 107 107 D->E: 3000-fold reduction in activity,
but no change in substrate affinity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 147 147 W->A: 24-fold reduction in activity, but
no change in substrate affinity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 147 147 W->F: 5-fold reduction in activity, but
no change in substrate affinity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 151 151 E->A: Loss of activity.
{ECO:0000269|PubMed:9484229}.
MUTAGEN 155 155 K->A: Loss of activity.
{ECO:0000269|PubMed:9484229}.
CONFLICT 118 119 IA -> MP (in Ref. 3; CAA46561).
{ECO:0000305}.
STRAND 2 7 {ECO:0000244|PDB:1QR0}.
HELIX 14 21 {ECO:0000244|PDB:1QR0}.
HELIX 26 34 {ECO:0000244|PDB:1QR0}.
HELIX 38 58 {ECO:0000244|PDB:1QR0}.
HELIX 63 65 {ECO:0000244|PDB:1QR0}.
STRAND 85 91 {ECO:0000244|PDB:1QR0}.
STRAND 94 102 {ECO:0000244|PDB:1QR0}.
STRAND 105 110 {ECO:0000244|PDB:1QR0}.
HELIX 116 119 {ECO:0000244|PDB:1QR0}.
STRAND 120 123 {ECO:0000244|PDB:1QR0}.
HELIX 125 133 {ECO:0000244|PDB:1QR0}.
HELIX 136 157 {ECO:0000244|PDB:1QR0}.
HELIX 160 162 {ECO:0000244|PDB:4MRT}.
HELIX 165 167 {ECO:0000244|PDB:4MRT}.
STRAND 169 172 {ECO:0000244|PDB:1QR0}.
HELIX 174 176 {ECO:0000244|PDB:1QR0}.
STRAND 178 181 {ECO:0000244|PDB:1QR0}.
STRAND 190 194 {ECO:0000244|PDB:1QR0}.
STRAND 200 209 {ECO:0000244|PDB:1QR0}.
HELIX 220 224 {ECO:0000244|PDB:1QR0}.
SEQUENCE 224 AA; 26168 MW; 0FEFB5D9D3534C68 CRC64;
MKIYGIYMDR PLSQEENERF MSFISPEKRE KCRRFYHKED AHRTLLGDVL VRSVISRQYQ
LDKSDIRFST QEYGKPCIPD LPDAHFNISH SGRWVICAFD SQPIGIDIEK TKPISLEIAK
RFFSKTEYSD LLAKDKDEQT DYFYHLWSMK ESFIKQEGKG LSLPLDSFSV RLHQDGQVSI
ELPDSHSPCY IKTYEVDPGY KMAVCAAHPD FPEDITMVSY EELL


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