ID   OLSA_BRUA2              Reviewed;         267 AA.
AC   Q2YQS9;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Lyso-ornithine lipid O-acyltransferase {ECO:0000305};
DE            EC=2.3.1.270 {ECO:0000269|PubMed:21249206};
GN   Name=olsA {ECO:0000303|PubMed:21249206};
GN   OrderedLocusNames=BAB1_2153 {ECO:0000312|EMBL:CAJ12109.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=2308;
RX   PubMed=21249206; DOI=10.1371/journal.pone.0016030;
RA   Palacios-Chaves L., Conde-Alvarez R., Gil-Ramirez Y., Zuniga-Ripa A.,
RA   Barquero-Calvo E., Chacon-Diaz C., Chaves-Olarte E., Arce-Gorvel V.,
RA   Gorvel J.P., Moreno E., de Miguel M.J., Grillo M.J., Moriyon I.,
RA   Iriarte M.;
RT   "Brucella abortus ornithine lipids are dispensable outer membrane
RT   components devoid of a marked pathogen-associated molecular pattern.";
RL   PLoS ONE 6:e16030-e16030(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:0000269|PubMed:21249206}.
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:21249206};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55761;
CC         Evidence={ECO:0000269|PubMed:21249206};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000269|PubMed:21249206}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant lacks ornithine lipids but
CC       synthesizes a component corresponding to the lyso-ornithine lipid
CC       precursor. It does not affect resistance to bactericidal peptides or
CC       permeability of the outer membrane. {ECO:0000269|PubMed:21249206}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. OlsA subfamily. {ECO:0000305}.
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DR   EMBL; AM040264; CAJ12109.1; -; Genomic_DNA.
DR   RefSeq; WP_002967046.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YQS9; -.
DR   STRING; 359391.BAB1_2153; -.
DR   EnsemblBacteria; CAJ12109; CAJ12109; BAB1_2153.
DR   GeneID; 45125396; -.
DR   KEGG; bmf:BAB1_2153; -.
DR   PATRIC; fig|359391.11.peg.1388; -.
DR   HOGENOM; CLU_027938_0_2_5; -.
DR   OMA; PMLWVSN; -.
DR   PhylomeDB; Q2YQS9; -.
DR   Proteomes; UP000002719; Chromosome I.
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..267
FT                   /note="Lyso-ornithine lipid O-acyltransferase"
FT                   /id="PRO_0000452115"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   267 AA;  29662 MW;  3653ED60B2E7C702 CRC64;
     MIGTIRIFLV VAAMVALSLS LIPFQYLFLK LKNGWKRRLP NFFHRIVARL FGFRIRTVGK
     LHEGCPLLLV SNHTSWSDIV VLSAVGQVSF IAKSEVRDWP VFGMFAVLQR TVFVERARRG
     KTVHQTSEIA NRLIAGDAMV LFAEGTTSDG NRVLPFKTAL FGAAHAAIRE AGVAEVAVQP
     VAIAYTRVHG MAMGRYFRPL VSWPGDVELM PHLKGILREG AIDVEVRFGE PVFVTAETDR
     KALARTMENR VRALLQSALL GREIPEA