PLSB_PSE14
ID PLSB_PSE14 Reviewed; 833 AA.
AC Q48F46;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=PSPPH_3853;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000058; AAZ33585.1; -; Genomic_DNA.
DR RefSeq; WP_011169304.1; NC_005773.3.
DR AlphaFoldDB; Q48F46; -.
DR STRING; 264730.PSPPH_3853; -.
DR EnsemblBacteria; AAZ33585; AAZ33585; PSPPH_3853.
DR KEGG; psp:PSPPH_3853; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000000551; 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..833
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000049440"
FT MOTIF 309..314
FT /note="HXXXXD motif"
SQ SEQUENCE 833 AA; 94470 MW; 59081D4F9772858B CRC64;
MTRSPFRRLV FGTLRRLLYL WVRSETINQS SFTLNLDRSR PVFYALQSPS ISDLAVIDTE
CRKAGLPRPV LSVAVGNLIE PAAFFYLTPA PDWLGRQDKR GAPPTLERLV AAVSQNPGED
AQIIPVSVFW GQSPDRESSA WKLLFADSWA VTGRLRRLVS ILILGRKTRV QFSAPIHMRE
LVGENKGYEL TLRMTQRLLR VHFRNLKSAV IGPDVSHRRT VVKGLLDEPL VKQAIIEEAE
RENITQDKAR DRALSYGNEI ASDYTYSVIR FMEVVLSWFW NKIYDGIKVS HIEGVQEVAP
GHEVIYVPCH RSHIDYLLLS YLLFCNGLTP PHIAAGINLN MPVVGSLLRR GGAFFMRRTF
KGNPLYTAVF TEYLHTLFIK GFPVEYFVEG GRSRTGRMLQ PKTGMLAITL RSFLRNSRMP
IVFVPLYIGY ERVLEGRTYL GELRGATKKK ESIFDIFKVI GALKQRFGQV SVNFGAPIKL
AEFLDGEQPD WREQALAPQF RPEWLSETTH RLGERVAQHL NEAAAVNPMN LVAVALLSTQ
RLALDDQAME RVLDLYLTLL RAVPYSPHTT LPEGDGRSLI EHVKGMDLLA EQKDALGKIL
YLNEQNAVLM TYYRNNVLHI FALPSLLASF FQSSSRMSRE QILRYTRALY PFLQSELFIR
WPLSELDEVV DQWLAAFVEQ GLLRFKKDVY VRPEPSSREF VLLTLLSRAI AQTLQRFYMA
IALLLNSGQN TLSAEQLEDL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDLGVLRK
DSAGKLSYHP MLGELAEGAA KRVLPAEIRL SIRQVALHSN EEEQDAGNGE GVA
