PLSB_YERPN
ID PLSB_YERPN Reviewed; 825 AA.
AC Q1CE96; C4GY76;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393}; OrderedLocusNames=YPN_3357;
GN ORFNames=YP516_3815;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00393};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000255|HAMAP-Rule:MF_00393}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
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:0000255|HAMAP-Rule:MF_00393}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC Rule:MF_00393}.
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DR EMBL; CP000305; ABG19684.1; -; Genomic_DNA.
DR EMBL; ACNQ01000017; EEO75876.1; -; Genomic_DNA.
DR RefSeq; WP_002214644.1; NZ_ACNQ01000017.1.
DR AlphaFoldDB; Q1CE96; -.
DR SMR; Q1CE96; -.
DR EnsemblBacteria; ABG19684; ABG19684; YPN_3357.
DR GeneID; 57974292; -.
DR KEGG; ypn:YPN_3357; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000008936; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR HAMAP; MF_00393; Glyc3P_acyltrans; 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.
DR TIGRFAMs; TIGR03703; plsB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..825
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000049472"
FT REGION 803..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 304..309
FT /note="HXXXXD motif"
SQ SEQUENCE 825 AA; 93621 MW; 0D0C9A0CDC751127 CRC64;
MSGWRKIYYK LLNLPLKLLV KSKVIPADPV SELGLDPSRP ILYVLPYNSK ADLLTLRAQC
LAQDLPDPLI PLEIDGVQLP SHVFIENGPR VFRYYVPKQE SVKLFHDYLD LHRNNPALDI
QMLPVSVMFG RSPGREGHGT PHLRVLNGVQ KFFAVLWLGR DSFVRFSTTV SLRRMASEHG
TDKTIAHKLA RVARMHFSRQ RLAAVGPSLP ARQDLFKKLL ASKAIEKAVA DEARSKKISH
EKAQQNAITL MEEIAANFSY EAVRLSDRVL SWTWNRLYQG INVHNAERVR QLAQDGHEIV
YVPCHRSHMD YLLLSYVLYH QGLVPPHIAA GINLNFWPAG PIFRRLGAFF IRRTFKGNKL
YSTVFREYLG ELFTRGYSVE YFVEGGRSRT GRLLEPKTGT LSMTIQAMLR GGTRPITLVP
IYIGYEHVME VGTYAKELRG AIKEKENLLQ MLRGLRKLRN LGQGYVNFGE PLPLTTYLNT
HVPQWRDAID PIEAQRPSWL TPAVNDLANQ IMVRINNAAA ANAMNLCSTA LLASRQRSLT
REQLLEQLDC YLQLMRNAPY AKDTTVPDKT PEELLNHALN MNKFEVEKDT IGDIIILPRE
QAVLMTYYRN NIQHLLILPS LIASMVMYHR RITRTELLHK ISMIYPMLKA ELFLHYSKEQ
LPETLDTLID ELARQQLICD KGSELVLNPA RIRPLQLLAA GVRETLQRYA ITLSLLSATP
SINRGALEKE SRIMAQRLSV LHGINAPEFF DKAVFSTLVA TLREEGYISD SGDAIQEHTL
EVYNMLSALM TPEVKLTIES VSMPAETSNQ PEAPETPEPE GKTES
