SFP_BACSU
ID SFP_BACSU Reviewed; 224 AA.
AC P39135;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=4'-phosphopantetheinyl transferase Sfp;
DE EC=2.7.8.7 {ECO:0000269|PubMed:11451672, ECO:0000269|PubMed:9484229};
DE AltName: Full=Surfactin synthase-activating enzyme;
GN Name=sfp; Synonyms=lpa-8; OrderedLocusNames=BSU03570;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-14.
RC STRAIN=168, and oKB105;
RX PubMed=1557038; DOI=10.1007/bf00280011;
RA Nakano M.M., Corbell N., Besson J., Zuber P.;
RT "Isolation and characterization of sfp: a gene that functions in the
RT production of the lipopeptide biosurfactant, surfactin, in Bacillus
RT subtilis.";
RL Mol. Gen. Genet. 232:313-321(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8407792; DOI=10.1128/jb.175.19.6203-6211.1993;
RA Grossman T.H., Tuckman M., Ellestad S., Osburne M.S.;
RT "Isolation and characterization of Bacillus subtilis genes involved in
RT siderophore biosynthesis: relationship between B. subtilis sfpo and
RT Escherichia coli entD genes.";
RL J. Bacteriol. 175:6203-6211(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH624, and ATCC 21332 / IAM 1213;
RX PubMed=8355609; DOI=10.1111/j.1365-2958.1993.tb01629.x;
RA Cosmina P., Rodriguez F., de Ferra F., Grandi G., Perego M., Venema G.,
RA van Sinderen D.;
RT "Sequence and analysis of the genetic locus responsible for surfactin
RT synthesis in Bacillus subtilis.";
RL Mol. Microbiol. 8:821-831(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YB8;
RX PubMed=8639027; DOI=10.1007/s002030050322;
RA Tsuge K., Ano T., Shoda M.;
RT "Isolation of a gene essential for biosynthesis of the lipopeptide
RT antibiotics plipastatin B1 and surfactin in Bacillus subtilis YB8.";
RL Arch. Microbiol. 165:243-251(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [7]
RP FUNCTION.
RX PubMed=8939709; DOI=10.1016/s1074-5521(96)90181-7;
RA Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M.,
RA Marahiel M.A., Reid R., Khosla C., Walsh C.T.;
RT "A new enzyme superfamily -- the phosphopantetheinyl transferases.";
RL Chem. Biol. 3:923-936(1996).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLY-105; ASP-107; TRP-147; GLU-151 AND LYS-155.
RX PubMed=9484229; DOI=10.1021/bi9719861;
RA Quadri L.E.N., Weinreb P.H., Lei M., Nakano M.M., Zuber P., Walsh C.T.;
RT "Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl
RT transferase for peptidyl carrier protein domains in peptide synthetases.";
RL Biochemistry 37:1585-1595(1998).
RN [9]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11451672; DOI=10.1016/s1074-5521(01)00047-3;
RA Sanchez C., Du L., Edwards D.J., Toney M.D., Shen B.;
RT "Cloning and characterization of a phosphopantetheinyl transferase from
RT Streptomyces verticillus ATCC15003, the producer of the hybrid peptide-
RT polyketide antitumor drug bleomycin.";
RL Chem. Biol. 8:725-738(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10581256; DOI=10.1093/emboj/18.23.6823;
RA Reuter K., Mofid M.R., Marahiel M.A., Ficner R.;
RT "Crystal structure of the surfactin synthetase-activating enzyme sfp: a
RT prototype of the 4'-phosphopantetheinyl transferase superfamily.";
RL EMBO J. 18:6823-6831(1999).
CC -!- FUNCTION: Activates the seven peptidyl carrier protein (PCP) domains of
CC the first three subunits (SrfAA, SrfAB and SrfAC) of surfactin
CC synthetase by transferring the 4'-phosphopantetheinyl moiety of
CC coenzyme A (CoA) to a serine residue. Required for cells of B.subtilis
CC to become producers of the lipopeptide antibiotics surfactin and
CC plipastatin B1. {ECO:0000269|PubMed:8939709,
CC ECO:0000269|PubMed:9484229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC Evidence={ECO:0000269|PubMed:11451672, ECO:0000269|PubMed:9484229};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 uM for coenzyme A {ECO:0000269|PubMed:9484229};
CC KM=1.3 uM for a peptide fragment encompassing residues 960-1084 of
CC surfactin synthetase SrfAB subunit {ECO:0000269|PubMed:9484229};
CC KM=1.8 uM for a peptide fragment encompassing residues 2006-2123 of
CC surfactin synthetase SrfAB subunit {ECO:0000269|PubMed:9484229};
CC KM=3.7 uM for Streptomyces mobaraensis apo-PCP BlmI
CC {ECO:0000269|PubMed:11451672};
CC KM=11 uM for Streptomyces glaucescens apo-ACP TcmM
CC {ECO:0000269|PubMed:11451672};
CC Note=kcat is 104 min(-1) with a peptide fragment encompassing
CC residues 960-1084 of surfactin synthetase SrfAB subunit as substrate.
CC kcat is 56 min(-1) with a peptide fragment encompassing residues
CC 2006-2123 of surfactin synthetase SrfAB subunit as substrate
CC (PubMed:9484229). kcat is 7.2 min(-1) with S.mobaraensis apo-PCP BlmI
CC as substrate and 0.89 min(-1) with S.glaucescens apo-ACP TcmM as
CC substrate (PubMed:11451672). {ECO:0000269|PubMed:11451672,
CC ECO:0000269|PubMed:9484229};
CC pH dependence:
CC Optimum pH is 6.0. Displays less than 20% of Vmax at both pH 5.0 and
CC pH 7.0. {ECO:0000269|PubMed:9484229};
CC -!- SUBUNIT: Monomer in solution.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
CC -!- CAUTION: Strain 168 and its derivatives encode a truncated, inactive
CC version of this protein. The sequence shown here corresponds to that of
CC strain ATCC 21332 which is active. {ECO:0000305}.
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DR EMBL; X63158; CAA44858.1; -; Genomic_DNA.
DR EMBL; X65610; CAA46561.1; -; Genomic_DNA.
DR EMBL; L17438; AAC36829.1; -; Unassigned_DNA.
DR EMBL; X70356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D50562; BAA09125.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12151.2; -; Genomic_DNA.
DR PIR; S20463; S20463.
DR PDB; 1QR0; X-ray; 1.90 A; A=1-224.
DR PDB; 4MRT; X-ray; 2.00 A; A=1-224.
DR PDBsum; 1QR0; -.
DR PDBsum; 4MRT; -.
DR AlphaFoldDB; P39135; -.
DR SMR; P39135; -.
DR DrugBank; DB01992; Coenzyme A.
DR PaxDb; P39135; -.
DR PRIDE; P39135; -.
DR InParanoid; P39135; -.
DR BioCyc; MetaCyc:MON-13919; -.
DR BRENDA; 2.7.8.7; 658.
DR EvolutionaryTrace; P39135; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR GO; GO:1900192; P:positive regulation of single-species biofilm formation; IMP:CACAO.
DR Gene3D; 3.90.470.20; -; 2.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 2.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Direct protein sequencing;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..224
FT /note="4'-phosphopantetheinyl transferase Sfp"
FT /id="PRO_0000206077"
FT REGION 158..189
FT /note="Peptidyl carrier protein binding"
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT VARIANT 22
FT /note="S -> T (in strain: oKB105)"
FT VARIANT 97
FT /note="C -> G (in strain: oKB105)"
FT VARIANT 157..224
FT /note="EGKGLSLPLDSFSVRLHQDGQVSIELPDSHSPCYIKTYEVDPGYKMAVCAAH
FT PDFPEDITMVSYEELL -> GRQRLIASA (in strain: 168 and its
FT derivatives, non surfactin-producing strains)"
FT MUTAGEN 105
FT /note="G->A: Almost no activity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT MUTAGEN 105
FT /note="G->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT MUTAGEN 107
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT MUTAGEN 107
FT /note="D->E: 3000-fold reduction in activity, but no change
FT in substrate affinity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT MUTAGEN 147
FT /note="W->A: 24-fold reduction in activity, but no change
FT in substrate affinity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT MUTAGEN 147
FT /note="W->F: 5-fold reduction in activity, but no change in
FT substrate affinity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT MUTAGEN 151
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT MUTAGEN 155
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9484229"
FT CONFLICT 118..119
FT /note="IA -> MP (in Ref. 3; CAA46561)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 38..58
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1QR0"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1QR0"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1QR0"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1QR0"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4MRT"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4MRT"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1QR0"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1QR0"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1QR0"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:1QR0"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:1QR0"
SQ 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
