ID   PLBAC_BACSU             Reviewed;         259 AA.
AC   O34705; Q795P7;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Phospholipase YtpA;
DE            EC=3.1.1.-;
DE   AltName: Full=Bacilysocin biosynthesis protein YtpA;
GN   Name=ytpA; OrderedLocusNames=BSU30510;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(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 BACILYSOCIN SYNTHESIS, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=11796336; DOI=10.1128/aac.46.2.315-320.2002;
RA   Tamehiro N., Okamoto-Hosoya Y., Okamoto S., Ubukata M., Hamada M.,
RA   Naganawa H., Ochi K.;
RT   "Bacilysocin, a novel phospholipid antibiotic produced by Bacillus subtilis
RT   168.";
RL   Antimicrob. Agents Chemother. 46:315-320(2002).
CC   -!- FUNCTION: Phospholipase involved in the biosynthesis of the antibiotic
CC       bacilysocin. It probably catalyzes the hydrolysis of the 2-sn-acyl
CC       moiety of phosphatidylglycerol to produce bacilysocin
CC       (lysophosphatidylglycerol). Is also able to catalyze the hydrolysis
CC       reaction of one acyl bond in phosphatidylcholine in vitro (actual
CC       cleavage point is unknown), resulting in lysophosphatidylcholine.
CC       {ECO:0000269|PubMed:11796336}.
CC   -!- PATHWAY: Antibiotic biosynthesis; bacilysocin biosynthesis.
CC       {ECO:0000269|PubMed:11796336}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene entirely lose the ability
CC       to produce bacilysocin and display a 10-fold reduction in the ability
CC       to form spores. {ECO:0000269|PubMed:11796336}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AF008220; AAC00245.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15029.1; -; Genomic_DNA.
DR   PIR; D69998; D69998.
DR   RefSeq; NP_390929.1; NC_000964.3.
DR   RefSeq; WP_004398545.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34705; -.
DR   SMR; O34705; -.
DR   STRING; 224308.BSU30510; -.
DR   ESTHER; bacsu-YTPA; Monoglyceridelipase_lysophospholip.
DR   PaxDb; O34705; -.
DR   EnsemblBacteria; CAB15029; CAB15029; BSU_30510.
DR   GeneID; 937237; -.
DR   KEGG; bsu:BSU30510; -.
DR   PATRIC; fig|224308.179.peg.3309; -.
DR   eggNOG; COG2267; Bacteria.
DR   InParanoid; O34705; -.
DR   OMA; FHGFSDH; -.
DR   PhylomeDB; O34705; -.
DR   BioCyc; BSUB:BSU30510-MON; -.
DR   UniPathway; UPA01001; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR022742; Hydrolase_4.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Hydrolase; Reference proteome; Serine esterase.
FT   CHAIN           1..259
FT                   /note="Phospholipase YtpA"
FT                   /id="PRO_0000386473"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        236
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
SQ   SEQUENCE   259 AA;  29566 MW;  1D75C1841514E7F9 CRC64;
     MWTWKADRPV AVIVIIHGAS EYHGRYKWLI EMWRSSGYHV VMGDLPGQGT TTRARGHIRS
     FQEYIDEVDA WIDKARTFDL PVFLLGHSMG GLVAIEWVKQ QRNPRITGII LSSPCLGLQI
     KVNKALDLAS KGLNVIAPSL KVDSGLSIDM ATRNEDVIEA DQNDSLYVRK VSVRWYRELL
     KTIESAMVPT EAFLKVPLLV MQAGDDKLVD KTMVIKWFNG VASHNKAYRE WEGLYHEIFN
     EPEREDVFKA ARAFTDQYI