ID   PPSA_BACSU              Reviewed;        2561 AA.
AC   P39845;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Plipastatin synthase subunit A;
DE            EC=2.3.1.-;
DE   AltName: Full=Peptide synthase 1;
DE   Includes:
DE     RecName: Full=ATP-dependent glutamate adenylase 1;
DE              Short=GluA 1;
DE     AltName: Full=Glutamate activase 1;
DE   Includes:
DE     RecName: Full=ATP-dependent ornithine adenylase;
DE              Short=OrnA;
DE     AltName: Full=Ornithine activase;
GN   Name=ppsA; Synonyms=pps1; OrderedLocusNames=BSU18340;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [2]
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   [3]
RP   SEQUENCE REVISION TO 916.
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   [4]
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 Orn as part of the biosynthesis
CC       of the lipopeptide antibiotic lipastatin. The Orn residue is further
CC       epimerized to the D-isomer form. The activation sites for these amino
CC       acids consist of individual domains. {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; Z34883; CAA84360.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13717.2; -; Genomic_DNA.
DR   PIR; I40456; I40456.
DR   RefSeq; NP_389716.2; NC_000964.3.
DR   RefSeq; WP_009967358.1; NZ_CM000487.1.
DR   RefSeq; WP_010886523.1; NZ_CP053102.1.
DR   AlphaFoldDB; P39845; -.
DR   SMR; P39845; -.
DR   STRING; 224308.BSU18340; -.
DR   PaxDb; P39845; -.
DR   PRIDE; P39845; -.
DR   EnsemblBacteria; CAB13717; CAB13717; BSU_18340.
DR   GeneID; 939983; -.
DR   KEGG; bsu:BSU18340; -.
DR   PATRIC; fig|224308.179.peg.2001; -.
DR   eggNOG; COG1020; Bacteria.
DR   InParanoid; P39845; -.
DR   OMA; RVWFTEL; -.
DR   BioCyc; BSUB:BSU18340-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; 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   Gene3D; 1.10.1200.10; -; 2.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.559.10; -; 3.
DR   InterPro; IPR010071; AA_adenyl_domain.
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..2561
FT                   /note="Plipastatin synthase subunit A"
FT                   /id="PRO_0000193185"
FT   DOMAIN          961..1036
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2007..2081
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          1..1038
FT                   /note="Domain 1 (glutamate-activating)"
FT   REGION          2..300
FT                   /note="Condensation 1"
FT   REGION          485..888
FT                   /note="Adenylation 1"
FT   REGION          1048..2554
FT                   /note="Domain 2 (D-ornithine-activating)"
FT   REGION          1048..1338
FT                   /note="Condensation 2"
FT   REGION          1525..1932
FT                   /note="Adenylation 2"
FT   REGION          2089..2554
FT                   /note="Epimerization"
FT   MOD_RES         996
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2042
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   CONFLICT        916
FT                   /note="E -> Q (in Ref. 1; CAA84360)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2561 AA;  289185 MW;  3130D78EC107DDBC CRC64;
     MSEHTYSLTH AQRRVWFTEL LEPDTSICNL TACVKFKGNI ELDTLEGALN HSISRNDAIR
     FQLLEGEELE PRLHLTEYKY YPLRIIDFSN VEMIEIEQWI QDQASIPFKL FNSPLFQFYL
     LRIDSHEVWL FAKFHHIIMD GISLNVMGNQ IIDLYQKMKK KDPLPDQPEP SYLSYIEKES
     QYLQSPRFAK DRLFWTQTFE HPLEYHSLAD QTSLQKQSTS ASRDTIILSP DLEQTIRIFC
     EEHKINIISL FMASFYICIS RITSKKDLAI GTYYGNRGSK AEKEMLGMFV SSLPIRITVD
     PDTDFLSFVR TIGREQLSVM RHQRFPYNLL VNELRNEQKD LHNLIGISMQ YQPLQWHNAD
     DFDYETALYF SGYTANELSV QIQERIDNGT IQLNFDYQNT LFSLEDIKRI QSHLLTILEN
     ALKHPHSFIR ELDMTNTREK QKLLYEFNKT EAVSPKAFTL HGLFERQAAF TPERLAIRFS
     GGSLTYAELD MYASRLAAHL AARGVTNESI VGVLSERSPD MLIAVLAVLK AGGAYLPLDP
     AYPKERLSYM LKDSGASLLL TQPGCSAPNF SGETLEVDMT SLASEKAENH EFTPADGGSL
     AYVIYTSGST GQPKGVAVEH RQAVSFLTGM QHQFPLSEDD IVMVKTSFSF DASVWQLFWW
     SLSGASAYLL PPGWEKDSAL IVQAIHQENV TTAHFIPAML NSFLDQAEIE RLSDRTSLKR
     VFAGGEPLAP RTAARFASVL PQVSLIHGYG PTEATVDAAF YVLDPERDRD RLRIPIGKPV
     PGARLYVLDP HLAVQPSGVA GELYIAGAGV ARGYLNRPAL TEERFLEDPF YPGERMYKTG
     DVARWLPDGN VEFLGRTDDQ VKIRGYRIEP GEIEAALRSI EGVREAAVTV RTDSGEPELC
     AYVEGLQRNE VRAQLERLLP GYMVPAYMIE MEQWPVTPSG KLDRNALPAP GGAADAETYT
     APRNVTEMKL SQLWEDVLKN GPVGIHDNFF DRGGHSLKAT ALVSRIAKEF DVQVPLKDVF
     AHPTVEGLAT VIREGTDSPY EAIKPAEKQE TYPVSSAQKR IYVLQQLEDG GTGYNMPAVL
     ELEGKLNPER MERAFKELIK RHESLRTSFE QDAGGDPVQR IHDEVPFTLQ TTVLGERTEQ
     EAAAAFIKPF DLSQAPLFRA QIVKISDERH LLLVDMHHII SDGVSVNILI REFGELYNNR
     NLPALRIQYK DYAVWREGFK TGDAYKTQEA YWLKQLEGEL PVLDLPADHA RPPVRSFAGD
     KVSFTLDQEV ASGLHKLARE NGSTLYMVLL AAYTAFLSRL SGQEDIIVGS PIAGRPHKDL
     EPILGMFVNT LALRTRPEGG KPFVQYLQEV RETALEAFEH QDYPFEELVD KLELTRDMSR
     NPVFDAMFIL QNVEKQDIDL REIKVRPANF AHHISLFDIT LIATEISGSI CCEMEFSTEV
     FLKATIERWA DHFIEFLHEA LSTPETSLAQ INILSDKEKQ KIVFEFNKTQ VEFAQKDIPF
     HRIFEAKAEE NPEHIAVIDN ETEISYRLLN ERANRLARTL QNRKGPKPTV AVLAKRSIDA
     IVGVLAVMKA GGVYIPIDAH YPKARIEYIL RDSGADILLL QRELKHLISN SPESEMSHIF
     LDDEGSFEES NCNLNLSPAP EEPVYIIYTS GTTGAPKGVI VTYQNFTHAA LAWRQIYELD
     RKPVRLLQIA SFSFDVFSGD LARTLTNGGT LIVCPDETRL EPAEIYKIIK SQRITVMEST
     PALIIPVMEY VYRNQFKLPD LDILILGSDM VKAQDFKTLT DRFGQSMRII NSYGVTEATI
     DSSFYETSMG GECTGDNVPI GSPLPNVHMY VLSQTDQIQP IGVAGELCIG GAGVAKGYHH
     KPDLTQMKFT ENPFVSGERL YRTGDRACWL PNGTIRLLGR MDYQVKINGY RIETEEIESV
     LLQTGLVREA AVAVQHDKNG QAGLAAYIVP SDVNTNALRA ALTKELPAYM IPAYLIPLVN
     MPLTLNGKLD RNALPAPNNV LSRPYTAPVN DLQKTMAYIW EDVLSMSRVG IHDSFFELGG
     DSIKALQVAA RLAAEGWSMT IRDLFRYSTI QELCGHITPL ASQADQGPAE GEAELTPIQR
     RFFGQVHAFH YHYNQSVMLF SEKGFNANAL HLALRKITEH HDAIRMIFQR DQNGHVIQFN
     RGINHKDHEL FGLYISDWTK ASLERAHLDE KLAAEETVIQ SKMNVEKGPL LQAGLFKTAE
     GDHLLIALHH LVIDGVSWRI LLEDLAAAYQ QALEKKEIQL PPKTDSYLSY ADGLTQIAES
     KQLLSEKTYW QTILDAHTAF LPKDIENVPD KLQMNSDAAA FVLSGDWTEK LLFETQQAYG
     TDANELLLTA LGMALSEWTG HDQIVISTEG HGREGHVPNI DISRTVGWFT SIYPILLDMG
     IPEPFEDQLA YRIKTTKDML RRVPNKGTGY GLLTHIGELR HKEPEVSFNY LGQFSEEKEV
     ETFQLSYYQP RYEIAGERER EYELDINALI TDGRLHVKAV YTQVFSKHSI ECFMDRFHRH
     LIETIEHCSQ KKAREKTLSD FSNKELTLSA LSSIEDLVKD L