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 27-MAR-2024, entry version 93.
DE RecName: Full=Putative acyltransferase plsB1;
GN Name=plsB1; OrderedLocusNames=BQ2027_MB1577;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 PATRIC; fig|233413.5.peg.1723; -.
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; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 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.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell membrane; Membrane; Reference proteome; 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
//
