ID   PPSB_BACSU              Reviewed;        2560 AA.
AC   P39846;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Plipastatin synthase subunit B;
DE            EC=2.3.1.-;
DE   AltName: Full=Peptide synthase 2;
DE   Includes:
DE     RecName: Full=ATP-dependent tyrosine adenylase 1;
DE              Short=TyrA 1;
DE     AltName: Full=Tyrosine activase 1;
DE   Includes:
DE     RecName: Full=ATP-dependent threonine adenylase;
DE              Short=ThrA;
DE     AltName: Full=Threonine activase;
GN   Name=ppsB; Synonyms=pps2; OrderedLocusNames=BSU18330;
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   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 Tyr and Thr as part of the biosynthesis
CC       of the lipopeptide antibiotic plipastatin. The Thr residue is further
CC       converted to the D-allo-isomer form. The activation sites for these
CC       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; Z34883; CAA84361.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13716.1; -; Genomic_DNA.
DR   PIR; I40457; I40457.
DR   RefSeq; NP_389715.1; NC_000964.3.
DR   RefSeq; WP_003247155.1; NZ_JNCM01000027.1.
DR   AlphaFoldDB; P39846; -.
DR   SMR; P39846; -.
DR   STRING; 224308.BSU18330; -.
DR   PaxDb; P39846; -.
DR   PRIDE; P39846; -.
DR   EnsemblBacteria; CAB13716; CAB13716; BSU_18330.
DR   GeneID; 939993; -.
DR   KEGG; bsu:BSU18330; -.
DR   PATRIC; fig|224308.179.peg.2000; -.
DR   eggNOG; COG1020; Bacteria.
DR   InParanoid; P39846; -.
DR   OMA; LFDFWSH; -.
DR   PhylomeDB; P39846; -.
DR   BioCyc; BSUB:BSU18330-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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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..2560
FT                   /note="Plipastatin synthase subunit B"
FT                   /id="PRO_0000193186"
FT   DOMAIN          965..1040
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2006..2080
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          7..1042
FT                   /note="Domain 1 (tyrosine-activating)"
FT   REGION          7..310
FT                   /note="Condensation 1"
FT   REGION          496..889
FT                   /note="Adenylation 1"
FT   REGION          1052..2553
FT                   /note="Domain 2 (D-allo-threonine-activating)"
FT   REGION          1052..1342
FT                   /note="Condensation 2"
FT   REGION          1527..1927
FT                   /note="Adenylation 2"
FT   REGION          2088..2553
FT                   /note="Epimerization"
FT   MOD_RES         1000
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2041
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2560 AA;  290165 MW;  2DD2442D11B6E942 CRC64;
     MAQSAQIQDI YPLSHMQEGM LFHSLMDFSS KAYIEQTSFT ITGNLCVDSF QKSLNLLVSR
     YDIFRTIFIK EVPDLTGPQQ VVLSNRELTV YREDISRLAD QEQQTLIDAF MTKDREKGFD
     LQKDPLMRLA LFDRGDSQYT CVWTHHHIIM DGWCLGIILK EFFSMYDSLK NNSPVQLGST
     VPYSRYIEWL GEQDQEETAA YWSEYLKEYG NTASIPRIKR RTADGNYKAD QVSFSLAPDM
     VEKLTEAAQN WGVTLNTLFM SIWGVLLHRY NAADDAVFGS VISGRPSAID GIESMVGLFI
     NTVPVRIRSA EGITFSSLVK AVQEDILSSE QHGYYPLYEI QNHSPLKQGL IDHIFVFENY
     PVQLHQALSV ESENDEGALK LSDISMSEQT NYDFNIVIVP GESFYIKFSY NADVYEREEM
     LRIQGHLKQA LDCILTNPDV AVSDINIVPP EEQQVIQLFN ETERPYVNKT IPQLFEEQAH
     KTPEAAALKM GNECWTYRQL QVRANQIAHA LIEKGVGSGD IVAVMMGRSM EMPAALLGIW
     KAGGAYMPLD PHFPAERLSF LLKDSQAAQL LIEEDLISLI PPSYEGNTIT IEHTESYQTE
     APNMPPGDLA YLIYTSGTTG RPKGVLVDHH GIANTLQWRR EEYSMTEQDI SLHLFSYVFD
     GCVTSLFTPL LSGACVLLTT DDEAKDVLAL KRKIARYKVS HMIIVPSLYR VLLEVMTADD
     AKSLRIVTFA GEAVTPDLLE LNQIICPSAE LANEYGPTEN SVATTILRHL NKKERITIGH
     PIRNTKVFVL HGNQMQPIGA AGELCISGAG LARGYYKQQE LTQKAFSDHP FLEGERLYRT
     GDAGRFLPDG TIEYIGRFDD QVKIRGYRIE LREIETVLRQ APGVKEAAVL ARDVSAEEKE
     LVAYIVPEKG NSLPDLYQHL AGTLPSYMIP ASIINISQMP LTSSGKLDRF ALPEPENNTS
     VTYMAPRTLI EADLAHIWED VLNKQHIGIR DDFFQLGGQS LKAAALVSRI HKKLNVELPL
     SEVFSYPTVE SMAVKLMSLK EHAFTQIEPA DQRDVYPLSF SQKRLYALHQ LADDSTGYNM
     PAVLELRGNL NRQRLRSVLT ELVNRHEALR TVFVLDRDEP VQIIYPEMAF DLKELEMESE
     QMLESAIETF IKPFYLSSGP LFRACVITMG NNRGFLLLDM HHIIADGVSM STLVQEFTDL
     YCGKELPALN LHYKDFAVWQ QEKHPKELYK KQEAYWLGQL GGSLPTLELP LDKTRPRLPD
     FRGGTIEVNI DKDMADELHR LMAETGTTLY MILLAVYSIL LSKLSGQEDI VVGSPAAGRP
     HADLERVIGM FVNTLAMRSK PEGHKTFSSY LHDIRHLALT AYEHQDYPFE ELADKLDTNR
     EVNRNPLFDA MLVLQSSEDF RFEVPGLSIS SVTPKHDISK FDLTLHAEEH LSGIRCRFEY
     STALFEEETI TQWASYFIEL VKGVTADTEM RISNMQLLPA AERRLLLEKM GQYAAYPRNE
     NIVSLFEKQV AQYPEHIAVV CGHSQLTYRD LNEKAERAAA MLIKQGVRTG DIVGLMLDRS
     PDMIIGVLSI LKAGGAYLPI DPEYPKERIS FMLNDSGAKL LLTERGLNKP ADYTGHILYI
     DECENNSIPA DVNIEEIVTD QPAYVIYTSG TTGQPKGVIV EHRNVISLLK HQNLPFEFNH
     EDVWTLFHSY CFDFSVWEMF GALLNGSTLV VVSKETARDP QAFRLLLKKE RVTVLNQTPT
     AFYGLMLEDQ NHTDHLNIRY VIFGGEALQP GLLQSWNEKY PHTDLINMYG ITETTVHVTF
     KKLSAADIAK NKSNIGRPLS TLQAHVMDAH MNLQPTGVPG ELYIGGEGVA RGYLNRDELT
     ADRFVSNPYL PGDRLYRTGD LAKRLSNGEL EYLGRIDEQV KVRGHRIELG EIQAALLQYP
     MIKEAAVITR ADEQGQTAIY AYMVIKDQQA ANISDIRTYL KNALPDFMLP ARMIQIDSIP
     VTVNGKLDQK ALPEPEKQAY TADDISPRNE IETVMAEIWE ELLNVDELGV SANFFKLGGD
     SIKALQVCAR LKQRGFETTV REMFEHQTLG ELSARVRKDV RAIDQGPVEG EITWTPIQQW
     FFSQSLESHH FNQSVMIYRA ERFDEAALRK VLKSLVTHHD ALRIVCRHED GRQVQINRGI
     DLSDEELYAL ELFDVKDSLT EARNTIEEAA SRMQEHIRLE TGPLLHAGLF RTENGDHLFL
     TIHHLVVDAV SWRILFEDFS TAYKQAVSGE SIKLPQKTDS YLTYSQRIAD YSISRQVQRE
     AAYWDECENR HIQPIPKDND AASNTFKDTE VIDFELSRHH TELLLTAAHK AYSTEMNDIL
     LTALGLALQK WTGNNQFKIS MEGHGRESYL EDIDISRTVG WFTSIYPVWL DMRDSDHKDK
     EERLGHLIKQ TKDMLHRIPH KGAGYGVLKY ISKRWGSQKN SPEISFNYLG QFDQDIQSNA
     FEVSDIKPGN EISPNWERPY ALDISGAVSS GCLNMHIIYN RFQFEEKTIQ TFSRHFKQTL
     ENIIEHCTGK ENQEWSASDF TDEDLTLDEL SEIMGAVNKL