PLSB_PECCP
ID PLSB_PECCP Reviewed; 822 AA.
AC C6DKD0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=PC1_0512;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-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}.
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; CP001657; ACT11567.1; -; Genomic_DNA.
DR RefSeq; WP_012773220.1; NC_012917.1.
DR AlphaFoldDB; C6DKD0; -.
DR SMR; C6DKD0; -.
DR STRING; 561230.PC1_0512; -.
DR EnsemblBacteria; ACT11567; ACT11567; PC1_0512.
DR KEGG; pct:PC1_0512; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR OrthoDB; 580383at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002736; 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..822
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000205851"
FT REGION 803..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 306..311
FT /note="HXXXXD motif"
SQ SEQUENCE 822 AA; 93212 MW; FC3422144D095537 CRC64;
MSGWRKIYYK LLNLPLKLLV KSKVIPADPV VELGLDPSRP ILYVLPYNSQ ADLLTLRAKC
LALGLPDPSQ SFEFNGVELP SHVFINDGPR VFRYYVPKQK SVKLFHDYLD LHRANPDLDV
QMVPVSVMFG RSPGREGHSQ ATPHLRLLNG IEKFFAVLWL GRDSFVRFSS PVSLRYMATE
HGTDKTIAHK LARVARMHFS RQRLAAVGPR LPVRQELFNK LLDSKAIKKA VDDEARSKKI
SHEKAQQNAI ALMEEIAADF SYEAVRLSDR VLSWTWNRLY QGINVHNAER VRQLAQDGHG
IVYVPCHRSH MDYLLLSYVL YHQGLVPPHI AAGINLNFWP AGPIFRRLGA FFIRRTFKGN
KLYSTIFREY LGELFARGYS VEYFMEGGRS RTGRLLEPKT GTLAMTIQAM LRGGTRPITL
VPIYVGYEHV MEVGTYAKEL RGAVKEKEGF MQMVRGLRKL RNLGQGYVNF GEPLPLTTYL
NQHVPQWRDA IDPIEAQRPS WLTPTVQDIS MDIMVRINNS AAANAMNLCS TALLASRQRS
LTREQMQEQL DCYLQLLRQV PYHKDITVPK KTADELLEHA LSMNKFEVEK DSIGDIIILP
REQAVLMTYY RNNIQHLLVL PSLIASIVIH HRRITLAEVV RQIALIYPLL QSELFLHYSK
EQLPGVLETL ANELVQQQLL CSRDGELAIN PPRIRTLQLL SAGVRETLQR YAITLSLLCA
NPEINRGTLE KESRNMAQRL SVLHGINAPE FFDKAVFSTL VATLRTEGYI TDSAEAAQGD
IVAIYNILGD LITPEVRLTI ESASSSAEME AESQAVEETT QE
