ID   PLSB1_MYCTO             Reviewed;         621 AA.
AC   P9WI58; L0T8L2; P65734; Q10775;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Putative acyltransferase plsB1;
GN   Name=plsB1; OrderedLocusNames=MT1601;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45868.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45868.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70762; D70762.
DR   RefSeq; WP_003407762.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WI58; -.
DR   SMR; P9WI58; -.
DR   EnsemblBacteria; AAK45868; AAK45868; MT1601.
DR   KEGG; mtc:MT1601; -.
DR   PATRIC; fig|83331.31.peg.1723; -.
DR   HOGENOM; CLU_015407_1_0_11; -.
DR   Proteomes; UP000001020; 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_0000428064"
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