ID   OLSA_PSEAE              Reviewed;         258 AA.
AC   Q9HW50;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Lyso-ornithine lipid O-acyltransferase {ECO:0000305};
DE            EC=2.3.1.270 {ECO:0000250|UniProtKB:Q7APG1};
GN   Name=olsA {ECO:0000303|PubMed:21535098};
GN   OrderedLocusNames=PA4351 {ECO:0000312|EMBL:AAG07739.1};
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=21535098; DOI=10.1111/j.1574-6968.2011.02295.x;
RA   Lewenza S., Falsafi R., Bains M., Rohs P., Stupak J., Sprott G.D.,
RA   Hancock R.E.;
RT   "The olsA gene mediates the synthesis of an ornithine lipid in Pseudomonas
RT   aeruginosa during growth under phosphate-limiting conditions, but is not
RT   involved in antimicrobial peptide susceptibility.";
RL   FEMS Microbiol. Lett. 320:95-102(2011).
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:0000250|UniProtKB:Q7APG1}.
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:0000250|UniProtKB:Q7APG1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55761;
CC         Evidence={ECO:0000250|UniProtKB:Q7APG1};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000305|PubMed:21535098}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Induced under phosphate limiting conditions.
CC       {ECO:0000269|PubMed:21535098}.
CC   -!- DISRUPTION PHENOTYPE: Mutant shows no significant growth defect.
CC       {ECO:0000269|PubMed:21535098}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. OlsA subfamily. {ECO:0000305}.
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DR   EMBL; AE004091; AAG07739.1; -; Genomic_DNA.
DR   PIR; G83101; G83101.
DR   RefSeq; NP_253041.1; NC_002516.2.
DR   RefSeq; WP_003112769.1; NZ_QZGE01000004.1.
DR   AlphaFoldDB; Q9HW50; -.
DR   SMR; Q9HW50; -.
DR   STRING; 287.DR97_1528; -.
DR   PaxDb; Q9HW50; -.
DR   EnsemblBacteria; AAG07739; AAG07739; PA4351.
DR   GeneID; 881447; -.
DR   KEGG; pae:PA4351; -.
DR   PATRIC; fig|208964.12.peg.4556; -.
DR   PseudoCAP; PA4351; -.
DR   HOGENOM; CLU_027938_0_1_6; -.
DR   InParanoid; Q9HW50; -.
DR   OMA; PMLWVSN; -.
DR   PhylomeDB; Q9HW50; -.
DR   BioCyc; PAER208964:G1FZ6-4436-MON; -.
DR   PHI-base; PHI:3788; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IMP:PseudoCAP.
DR   GO; GO:0046467; P:membrane lipid biosynthetic process; IMP:PseudoCAP.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..258
FT                   /note="Lyso-ornithine lipid O-acyltransferase"
FT                   /id="PRO_0000452116"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  28305 MW;  470D3A69C993C4F2 CRC64;
     MARLRLLLRS ARLLGLVALG LGLAAWVSLR ERLPGADVTP LRQRLTRWWL ARLCAALPFE
     VRVSGEAPRQ PMLWVANHVS WTDIPLLGAL APLTFLSKAE VRAWPLAGWL AEKAGTLFIR
     RGSGDSRLIN QRLAEQLHRG RNLLIFPEGT TTNGESLRTF HGRLMASALE AGVAVQPVAI
     SYRRDGVPDA QAPFIGDDDL LSHLGRLLRG ERGSVHIQLL EPIPSQGLDR AELARQAQQA
     VRLALFGTAA PTQTRRAA