ID   PLSB1_MYCBO             Reviewed;         621 AA.
AC   P65735; A0A1R3XYN2; Q10775; X2BIP2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Putative acyltransferase plsB1;
GN   Name=plsB1; OrderedLocusNames=BQ2027_MB1577;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00180.1; -; Genomic_DNA.
DR   RefSeq; NP_855229.1; NC_002945.3.
DR   RefSeq; WP_003407762.1; NC_002945.4.
DR   AlphaFoldDB; P65735; -.
DR   SMR; P65735; -.
DR   EnsemblBacteria; SIU00180; SIU00180; BQ2027_MB1577.
DR   PATRIC; fig|233413.5.peg.1723; -.
DR   OMA; RFNLEWY; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR045520; GPAT_C.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Membrane; Transferase.
FT   CHAIN           1..621
FT                   /note="Putative acyltransferase plsB1"
FT                   /id="PRO_0000195245"
FT   MOTIF           123..128
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   621 AA;  69224 MW;  05E005BB5B6E241D CRC64;
     MTAREVGRIG LRKLLQRIGI VAESMTPLAT DPVEVTQLLD ARWYDERLRA LADELGRDPD
     SVRAEAAGYL REMAASLDER AVQAWRGFSR WLMRAYDVLV DEDQITQLRK LDRKATLAFA
     FSHRSYLDGM LLPEAILANR LSPALTFGGA NLNFFPMGAW AKRTGAIFIR RQTKDIPVYR
     FVLRAYAAQL VQNHVNLTWS IEGGRTRTGK LRPPVFGILR YITDAVDEID GPEVYLVPTS
     IVYDQLHEVE AMTTEAYGAV KRPEDLRFLV RLARQQGERL GRAYLDFGEP LPLRKRLQEM
     RADKSGTGSE IERIALDVEH RINRATPVTP TAVVSLALLG ADRSLSISEV LATVRPLASY
     IAARNWAVAG AADLTNRSTI RWTLHQMVAS GVVSVYDAGT EAVWGIGEDQ HLVAAFYRNT
     AIHILVDRAV AELALLAAAE TTTNGSVSPA TVRDEALSLR DLLKFEFLFS GRAQFEKDLA
     NEVLLIGSVV DTSKPAAAAD VWRLLESADV LLAHLVLRPF LDAYHIVADR LAAHEDDSFD
     EEGFLAECLQ VGKQWELQRN IASAESRSME LFKTALRLAR HRELVDGADA TDIAKRRQQF
     ADEIATATRR VNTIAELARR Q