ID   PPSC_BACSU              Reviewed;        2555 AA.
AC   P39847;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Plipastatin synthase subunit C;
DE            EC=2.3.1.-;
DE   AltName: Full=Peptide synthase 3;
DE   Includes:
DE     RecName: Full=ATP-dependent glutamate adenylase 2;
DE              Short=GluA 2;
DE     AltName: Full=Glutamate activase 2;
DE   Includes:
DE     RecName: Full=ATP-dependent alanine/valine adenylase;
DE              Short=Ala/ValA;
DE     AltName: Full=Alanine/valine activase;
GN   Name=ppsC; Synonyms=pps3; OrderedLocusNames=BSU18320;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-859.
RC   STRAIN=168;
RX   PubMed=7711903; DOI=10.1099/13500872-141-3-645;
RA   Tognoni A., Franchi E., Magistrelli C., Colombo E., Cosmina P., Grandi G.;
RT   "A putative new peptide synthase operon in Bacillus subtilis: partial
RT   characterization.";
RL   Microbiology 141:645-648(1995).
RN   [3]
RP   FUNCTION IN PLIPASTATIN BIOSYNTHESIS.
RX   PubMed=10471562; DOI=10.1128/aac.43.9.2183;
RA   Tsuge K., Ano T., Hirai M., Nakamura Y., Shoda M.;
RT   "The genes degQ, pps, and lpa-8 (sfp) are responsible for conversion of
RT   Bacillus subtilis 168 to plipastatin production.";
RL   Antimicrob. Agents Chemother. 43:2183-2192(1999).
CC   -!- FUNCTION: This protein is a multifunctional enzyme, able to activate
CC       and polymerize the amino acids Glu and Ala/Val as part of the
CC       biosynthesis of the lipopeptide antibiotic plipastatin. The Ala/Val
CC       residue is further epimerized to the D-isomer form. The activation
CC       sites for these amino acids consist of individual domains.
CC       {ECO:0000269|PubMed:10471562}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AL009126; CAB13715.1; -; Genomic_DNA.
DR   EMBL; Z34883; CAA84362.1; -; Genomic_DNA.
DR   PIR; C69681; C69681.
DR   RefSeq; NP_389714.1; NC_000964.3.
DR   RefSeq; WP_009967356.1; NZ_CP053102.1.
DR   AlphaFoldDB; P39847; -.
DR   SMR; P39847; -.
DR   IntAct; P39847; 16.
DR   STRING; 224308.BSU18320; -.
DR   PaxDb; P39847; -.
DR   PRIDE; P39847; -.
DR   EnsemblBacteria; CAB13715; CAB13715; BSU_18320.
DR   GeneID; 940102; -.
DR   KEGG; bsu:BSU18320; -.
DR   PATRIC; fig|224308.179.peg.1999; -.
DR   eggNOG; COG1020; Bacteria.
DR   InParanoid; P39847; -.
DR   OMA; AEACNFQ; -.
DR   BioCyc; BSUB:BSU18320-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.559.10; -; 3.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR   TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   Transferase.
FT   CHAIN           1..2555
FT                   /note="Plipastatin synthase subunit C"
FT                   /id="PRO_0000193187"
FT   DOMAIN          967..1042
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2003..2077
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          7..306
FT                   /note="Condensation 1"
FT   REGION          491..894
FT                   /note="Adenylation 1"
FT   REGION          1054..1344
FT                   /note="Condensation 2"
FT   REGION          1532..1927
FT                   /note="Adenylation 2"
FT   REGION          2085..2548
FT                   /note="Epimerization 3"
FT   MOD_RES         1002
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2038
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2555 AA;  287503 MW;  3E50B3395105D5D0 CRC64;
     MPQQPEIQDI YPLSFMQEGM LFHSLYDEQS RAYFEQASFT IHGQLDLERF QKSMDAVFDR
     YDIFRTAFIY KNVAKPRQVV LKQRHCPIHI EDISHLNERD KEHCTEAFKE QDKSKGFDLQ
     TDVLMRISIL KWAPDHYVCI WSHHHILMDG WCLGIVIKDF LHIYQALGKG QLPDLPPVQP
     YGTYIKWLMQ QDREEAAEYW KKRLQHFEKS TPLPKRTDQI PNGTLQQITF AIPEKETAEL
     QKIAAASGAT LNTVFQALWG IMLQKVNRSS DAVFGSVISG RPSELKDVEN MVGLFINTIP
     IRAQSDSLSF SDLVRRMQKD MNEAEAYSYF PLYDIQAQSA LKQELIDHII VFENTPTQQE
     IEELNQAGSF DFSVKDFEME EVTNYSCSVK VIPGRTLYVR IHFQTSAYQP SMMSEIKDYL
     LHMVSDVISD PSLPVSKMTL LDEDKTRKIV SQNNRTVSVS PEAPTLHGLF ERQAAVTPER
     LAIRFSGGSL TYAELDMYAS RLAAHLAARG VTNESIVGVL SERSPDMLIA VLAVLKAGGA
     YLPLDPAYPK ERLSYMLKDS GASLLLTQPG CSAPNFSGET LEVDMTSLEC EEVKRHVSAS
     VSDGSLAYVI YTSGSTGQPK GVAVEHRQAV SFLTGMQHQF RLSEDDIVMV KTSFSFDASV
     WQLFWWALSG ASAYLLPPGW EKDSALIVQA IHQENVTTAH FIPAMLNSFL DQAEIERLSD
     RTSLKRVFAG GEPLAPRTAA RFASVLPQVS LIHGYGPTEA TVDAAFYVLD PERDRDRLRI
     PIGKPVPGAR LYVLDPHLAV QPSGVAGELY IAGAGVARGY LNRPALTEER FLEDPFYLGE
     RMYKTGDVAR WLPDGNVEFL GRTDDQVKIR GYRIEPGEIE AALRSIEGVR EAAVTVRTDS
     GEPELCAYVE GLQRNEVRAQ LQRLLPGYMV PAYMIEMEQW PVTPSGKLDR NALPAPGGAA
     DAETYTAPRN VTEMKLSQLW EDVLKNGPVG IHDNFFDRGG HSLKATALVS RIAKEFDVQV
     PLKDVFAHPT VEGLATVIRE GTDSPYEAIK PAEKQETYPV SSAQKRIYVL QQLEDGGTGY
     NMPAVLELEG KLNLERMDRA FKELIKRHES LRTAFEQDAG GDPVQRIHDE VPFTLQTTVL
     GARTEEEAAA AFIKPFDLSQ APLFRAQIVK VSDERHLLLV DMHHIISDGV SVNILIREFG
     ELYNNRKLPA LRIQYKDYAV WQEGFKTGDA YKTQGAYWLK QLEGELPVLD LPADHARPPM
     RSFAGDKVSF TLDQEVTSGL YKLARENGST LYMVLLAAYT AFLSRLSGQE DIIVGSPIAG
     RPHKDLEPIL GMFVNTLALR TRPEGGKPFV QYLQEVRETA MEAFEHQDYP FEELVDKLEL
     TRDMSRNPLF DVMFVLQNMD QESLELDELC LKPAANNGHQ TSKFDLTLYA QEQPRGLLTF
     QMEFSTDLYK KKTIEKWLQY FNNMLLSIIK DNKAALGTIN ILNEDEAHYL IHELNRTKID
     YPRNETISRL FEMQAEQTPN AVAIVSDTQV FTYEDLNSWA NQIASVLQIK GVGPDSVVAL
     LTGRTPELIA GMLGILKAGG AYLPIDSNLP VERIAYMLSD SRAALLLQSE KTEKRLLGIE
     CEQIIIEDIQ KQGEAKNVES SAGPHSLAYI IYTSGSTGKP KGVMIEQRSV IRLVKNSNYI
     TFTPEDRLLM TSSIGFDVGS FEIFGPLLNG AALHLSDQQT FLDSHQLKRY IEHQGITTIW
     LTSSLFNHLT EQNEQTFSQL KHLIIGGEAL SPSHVNRIRN VCPEVSIWNG YGPTENTTFS
     TCLHIQKTYE LSIPIGRPVG NSTAFILNQW GVLQPVGAVG ELCVGGDGVA RGYLGRPDLT
     KEKFVPHPFA PGDRLYRTGD LARWLSDGTI EYVGRIDDQV KVRGYRVELG EIETALRQID
     GVKEAAVLAR TAQTGSKELF GYISVKAGTN AEQVRSLLAR SLPNYMIPAY IIEMETLPLT
     SNGKLNRKAL PEPDVASKQT YIPPRNELEE QLALIWQEVL GIQRIGIEDS FFELGGDSIK
     ALQVSARLGR YGLSLQVSDL FRHPKIKDLS PFIRKSERII EQGPIQGDVP WTPVQQWFFS
     QDIEERHHFN QSVMLFHSGR LSENALRPAL KKLAEHHDAL RMVYRNDDRR WIQINQGIHE
     SQLYSLRISD LSQSESGWET KIKQEVADLQ QSINLQEGPL LHAALFKTLT GDYLFLAIHH
     LVVDGVSWRI LLEDLSAGYQ QAAAGQTIQL PPKTDSYQEY ARRIQEYAQS SKLIREEAYW
     RSVEEQQAAE LPYEIPHHVN IDFSKRDSLS FSLTEADTAV LLQNVNHAYG TDTQDILLTA
     ASLAICEWTG GSKLRIAMEG HGREHILPEL DISRTVGWFT SMYPALISFE NHRDELGTSV
     KTVKDTLGRI PNKGVGYGML KYLTHPENKS ITFSKTPEIS FNYLGQFNDI ERQDTFRPSS
     LGSGKDITHT WKREQIIEMS AMAADKKLHF NLSYPPARFH RNTMEQLINR IEHFLLDIMK
     HCAGQQKAEK TLSDFSSQSL TAEDLDSISS LVEEL