OLSA_RHIME
ID OLSA_RHIME Reviewed; 292 AA.
AC Q7APG1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Lyso-ornithine lipid O-acyltransferase {ECO:0000305};
DE EC=2.3.1.270 {ECO:0000269|PubMed:12139618};
DE AltName: Full=Ornithine lipid synthesis protein A {ECO:0000305};
GN Name=olsA {ECO:0000303|PubMed:12139618};
GN ORFNames=SMc01116 {ECO:0000312|EMBL:CAC41841.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=1021;
RX PubMed=12139618; DOI=10.1046/j.1365-2958.2002.03043.x;
RA Weissenmayer B., Gao J.L., Lopez-Lara I.M., Geiger O.;
RT "Identification of a gene required for the biosynthesis of ornithine-
RT derived lipids.";
RL Mol. Microbiol. 45:721-733(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Catalyzes the second step in the formation of ornithine
CC lipids, which are phosphorus-free membrane lipids. Uses acyl-acyl
CC carrier protein (acyl-AcpP) as an acyl donor and converts lyso-
CC ornithine lipid (LOL) into ornithine lipid (OL).
CC {ECO:0000269|PubMed:12139618}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + a lyso-ornithine lipid = an N(2)-[(3R)-3-
CC (acyloxy)acyl]-L-ornithine lipid + holo-[ACP]; Xref=Rhea:RHEA:55760,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138482, ChEBI:CHEBI:138651, ChEBI:CHEBI:140663;
CC EC=2.3.1.270; Evidence={ECO:0000269|PubMed:12139618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55761;
CC Evidence={ECO:0000269|PubMed:12139618};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000269|PubMed:12139618}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant is deficient in the
CC biosynthesis of ornithine-derived lipids. It can still induce nitrogen-
CC fixing nodules on legume hosts, but it shows delayed nodulation if
CC compared to the wild type. {ECO:0000269|PubMed:12139618}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. OlsA subfamily. {ECO:0000305}.
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DR EMBL; AL591688; CAC41841.1; -; Genomic_DNA.
DR RefSeq; NP_384510.1; NC_003047.1.
DR RefSeq; WP_003527683.1; NC_003047.1.
DR AlphaFoldDB; Q7APG1; -.
DR SMR; Q7APG1; -.
DR STRING; 266834.SMc01116; -.
DR EnsemblBacteria; CAC41841; CAC41841; SMc01116.
DR GeneID; 61601883; -.
DR KEGG; sme:SMc01116; -.
DR PATRIC; fig|266834.11.peg.1777; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_0_1_5; -.
DR OMA; PMLWVSN; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..292
FT /note="Lyso-ornithine lipid O-acyltransferase"
FT /id="PRO_0000452117"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 258..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 292 AA; 32337 MW; F522E711810FAAA9 CRC64;
MINWVRVALC GMLLVMVSLV LMPVQILCLW LDLKPRRWLP RHWHRVACLL LGLRVRVHGE
LDRRRPLLLS ANHVSWKDIL VLSSVADVVF VAKSDVKSWP IFGLLARLQA SVFVEREQKR
TTGHQVNDIG RRLADGEIVV LFPEGTTSDG NRLLDIKTSL FGAAASAVPQ SPTGVVHVQP
LAISYTGIHG MPMGRYHRPI AAWPGDIGLV PHLLGVLREG ALEVDVDFGE AVDYDRHANR
KEVSRLIGQR IRKMLSDRLR GRSRSAAKGE PAPACSAAPD IPSDAQRSRL AP
