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 27-NOV-2024, entry version 155.
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; Bacillota; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_OZ025638.1.
DR AlphaFoldDB; P39847; -.
DR SMR; P39847; -.
DR IntAct; P39847; 16.
DR STRING; 224308.BSU18320; -.
DR PaxDb; 224308-BSU18320; -.
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 OrthoDB; 9765680at2; -.
DR BioCyc; BSUB:BSU18320-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd12117; A_NRPS_Srf_like; 1.
DR CDD; cd19543; DCL_NRPS; 1.
DR CDD; cd19534; E_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR FunFam; 3.30.300.30:FF:000010; Enterobactin synthetase component F; 2.
DR FunFam; 3.40.50.980:FF:000002; Enterobactin synthetase component F; 2.
DR FunFam; 3.30.559.10:FF:000012; Non-ribosomal peptide synthetase; 2.
DR FunFam; 3.40.50.12780:FF:000012; Non-ribosomal peptide synthetase; 2.
DR FunFam; 3.40.50.980:FF:000001; Non-ribosomal peptide synthetase; 2.
DR FunFam; 2.30.38.10:FF:000001; Non-ribosomal peptide synthetase PvdI; 2.
DR FunFam; 3.30.559.10:FF:000016; Nonribosomal peptide synthase Pes1; 1.
DR FunFam; 1.10.1200.10:FF:000005; Nonribosomal peptide synthetase 1; 2.
DR FunFam; 3.40.50.1820:FF:000818; Plipastatin synthase subunit C; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 4.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase_fold.
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_com.
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 NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR NCBIfam; TIGR01720; NRPS-para261; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
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 SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 6.
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
//
