PLSB_XYLFA
ID PLSB_XYLFA Reviewed; 870 AA.
AC Q9PEJ7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Glycerol-3-phosphate acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.15;
GN Name=plsB; OrderedLocusNames=XF_1031;
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
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 -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane 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; AE003849; AAF83841.1; -; Genomic_DNA.
DR PIR; B82732; B82732.
DR RefSeq; WP_010893550.1; NC_002488.3.
DR AlphaFoldDB; Q9PEJ7; -.
DR STRING; 160492.XF_1031; -.
DR EnsemblBacteria; AAF83841; AAF83841; XF_1031.
DR KEGG; xfa:XF_1031; -.
DR PATRIC; fig|160492.11.peg.1100; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000000812; 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; Reference proteome; Transferase.
FT CHAIN 1..870
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195241"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 351..356
FT /note="HXXXXD motif"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 98484 MW; 522A8DA99DFB9868 CRC64;
MPKKNSPLLP KETTPTQSSV DTSGSSNLTW PVSEHTIRRP LWARLLGQIL DPWLDLSIEP
EHCVQYPEHC VQYNDGRPII YVLEDYGLCN TLILDKACRK TKLPSPLIPL PGNPLQRKRA
YLALSRRSSS NSLIPNQRGG KTHSDSLANL LQAHRIRDTL DVHLVPVSIF IGRTPDRQSG
WFAVLFSENW ALVGRFRRLL AVLLNGRNTI VCFAPPISVR QTLNEGLPPE RTLRKLQRVL
RAHFRRIRET VIGPDLSTRR LLVDNVLATE AVREAIASQA KRDGTDLSET WRKAQAYAWE
IAADYSSPVI RSADFLFSHV WNRIYAGVLI HHVDSFKETA PGHEVVYVPS HRSHIDYLLL
SYCLYQCGIV LPHIVAGINL NLPIVGTLLR KCGAFFIRRS IKGNMLYSIV LSEYVAQLVA
GGYSLEYFIE GGRSRTGRLL QPKGGMIMMT LQAFLRQPRR PVLFQPIYIG YEKLIEGTSY
LDELSGEPKK KESIWRLFWN IPKVLKQKYG QVVVNFGEPI ALNDVLAELA PEWEGQALNE
NEKPAWLSNT VNHLARQIQT RINSAADVNP INLLALALLS TPKHAMGEAD LIAQITLCKK
ILLELPYSNR VTVTPHTPER IIAHAEQINI LTRVHHPLGD VLRVDGDNAV LLSYFRNNVL
HLFTASAWVA CCFKNNRRIS RIALIRLGVG MYPFLQAELF LPWTEDQFAQ HIQQVIELFV
REGLLLSAGD EEEDPLTRNT SQTDEVFRLR AISHSLQQAF ERYYITISIL VKNGPGTLSA
SELESLCQLA AQRLSLLYAS TAPEFFDKGL FRGFIQKLRE LNLVWPDTYS KLLFDERLDT
SAKDAQVILG RELRHTIERI SPEATKPAPK
