GENTAUR Molecular Products.

 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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 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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