ID   PPSE_BACSU              Reviewed;        1279 AA.
AC   O31827; Q799M0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Plipastatin synthase subunit E;
DE            EC=2.3.1.-;
DE   AltName: Full=Peptide synthase 5;
DE   Includes:
DE     RecName: Full=ATP-dependent isoleucine adenylase;
DE              Short=IsoA;
DE     AltName: Full=Isoleucine activase;
GN   Name=ppsE; Synonyms=pps5; OrderedLocusNames=BSU18300;
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=9387222; DOI=10.1099/00221287-143-11-3443;
RA   Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.;
RT   "Sequence completion, identification and definition of the fengycin operon
RT   in Bacillus subtilis 168.";
RL   Microbiology 143:3443-3450(1997).
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 acid Ile as part of the biosynthesis of the
CC       lipopeptide antibiotic plipastatin. The activation sites for this amino
CC       acid 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 1 phosphopantetheine covalently. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA74213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y13917; CAA74213.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB13713.1; -; Genomic_DNA.
DR   PIR; E69681; E69681.
DR   RefSeq; NP_389712.1; NC_000964.3.
DR   RefSeq; WP_010886522.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31827; -.
DR   SMR; O31827; -.
DR   STRING; 224308.BSU18300; -.
DR   ESTHER; bacsu-PPSE; Thioesterase.
DR   PaxDb; O31827; -.
DR   PRIDE; O31827; -.
DR   EnsemblBacteria; CAB13713; CAB13713; BSU_18300.
DR   GeneID; 939956; -.
DR   KEGG; bsu:BSU18300; -.
DR   PATRIC; fig|224308.43.peg.1940; -.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG3319; Bacteria.
DR   InParanoid; O31827; -.
DR   OMA; AFEWVER; -.
DR   PhylomeDB; O31827; -.
DR   BioCyc; BSUB:BSU18300-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: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; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.559.10; -; 1.
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; IPR020459; AMP-binding.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Multifunctional enzyme; Phosphopantetheine;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..1279
FT                   /note="Plipastatin synthase subunit E"
FT                   /id="PRO_0000360845"
FT   DOMAIN          975..1050
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          14..1047
FT                   /note="Domain (isoleucine-activating)"
FT   REGION          14..317
FT                   /note="Condensation"
FT   REGION          503..898
FT                   /note="Adenylation"
FT   REGION          1068..1273
FT                   /note="Thioesterase"
FT   MOD_RES         1010
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1279 AA;  144619 MW;  22EA638DEF0CEBE0 CRC64;
     MKKGADTMNT IKKIKNIYPL SHMQEGMLFH SFLRKEEGAY VEQSLFTIKG SLSYDWFQRS
     IQAIIDRHDI FRTVFLPHVP HLSGPRQVVM TEREFHLNSE DISHLPTNDQ NEYIERFKEK
     DKQKGFDLQK DMLMRISLFK TAKDEHVCIW SHHHILMDGW CLGIVMQEFM QIYQSIHAGK
     PLSLDPVRPY STYISWLTNR DKEKAAAYWD TYLKNYSAPS PLPRVSDKET KESYHREDLI
     FSLNKPLTDK LKETAKQHGV TLATLIQAVW GVMLQQYNRT DDVVFGAVVS GRPSEIPGVE
     QMIGLFINTI PIRIKTHQDE TFHELLIRCQ KEMLEAEPFT CQPLFDIQAN TALKQELIDH
     IIVFENYPLQ QKIADSADQT DSPLQIDQVQ VSEQSGYNFN LVVAPGEELV IKFSYNAFVY
     DAAWISCIKR QFTQALSTAA QHPHMPIADF SFLDATEKEQ IVTQFNNTKT EYPKNHTIID
     LFREQAEKTP DHTALVYGNM SISYKELDKR SNALARELIQ KGFRKNETAG ILAAHSPEFM
     ISVLAVLKAG GAYLPLDAEL PPERVSFMLE ETQAKMLIVQ KGLEQNAAFS GTCIISDAQG
     LMEENDIPIN ISSSPDDLAY IMYTSGSTGR PKGVMITNRN VVSLVRNSNY TSASGDDRFI
     MTGSISFDAV TFEMFGALLN GASLHIIDKS TMLTPDRFGA YLLENDITVL FLTTALFNQL
     AQVRADMFRG LHTLYVGGEA LSPALMNAVR HACPDLALHN IYGPTENTTF STFFEMKRDY
     AGPIPIGKPI SNSTAYILDT KGRLLPIGVP GELCVGGDGV AKGYLNRVDL TNAVFSPHPF
     LPGERIYRTG DLARWLPDGN LEYISRIDRQ MKIRGKRIEP AEIEARLLEM EGVQEAAVTL
     REKDGEAQLY THYVGDHKKT DTDFRADLAR VLPDYMIPQH WVRVERMPLT GNGKIDRSAL
     PIPENKPAKR QNIILPRNLV EEELANIWKQ VLGVNTISID DDFFAIGGHS LRALQVIHTL
     KHQQNIDIPI DFLFEHPTIA QLAEKLYSKQ LTAANEQHVI KLNQHGAQNL FCFPPISGFG
     IYFKDLALLL NEKAAVYGFH FIEQDTRIEQ YVNCMTDIQP EGPYVLLGYS AGGNLAFEVA
     QAMERKGLEV SDFIIVDAYL KEQPLPIDTG NDESAAYLPE AVREKVMKKK RNYQEYWAQL
     LNEGHIKASI HFIEAGIHPE TSGHTGLTKW EGACGNYSEY TGFGAHKDML EGTYAEKNAD
     IILDILEKIT SNQVILHKR