ID   OLSB_PSEAE              Reviewed;         251 AA.
AC   Q9HW51;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=L-ornithine N(alpha)-acyltransferase {ECO:0000305};
DE            EC=2.3.2.30 {ECO:0000250|UniProtKB:Q92SJ1};
GN   Name=olsB {ECO:0000303|PubMed:21535098};
GN   OrderedLocusNames=PA4350 {ECO:0000312|EMBL:AAG07738.1};
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   INDUCTION.
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 first step in the biosynthesis of ornithine
CC       lipids, which are phosphorus-free membrane lipids. Catalyzes the 3-
CC       hydroxyacyl-acyl carrier protein-dependent acylation of ornithine to
CC       form lyso-ornithine lipid (LOL). {ECO:0000250|UniProtKB:Q92SJ1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + L-ornithine = a lyso-ornithine
CC         lipid + H(+) + holo-[ACP]; Xref=Rhea:RHEA:20633, Rhea:RHEA-COMP:9685,
CC         Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78827, ChEBI:CHEBI:138482;
CC         EC=2.3.2.30; Evidence={ECO:0000250|UniProtKB:Q92SJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20634;
CC         Evidence={ECO:0000250|UniProtKB:Q92SJ1};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000250|UniProtKB:Q92SJ1}.
CC   -!- INDUCTION: Induced under phosphate limiting conditions.
CC       {ECO:0000269|PubMed:21535098}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. OlsB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG07738.1; -; Genomic_DNA.
DR   PIR; F83101; F83101.
DR   RefSeq; NP_253040.1; NC_002516.2.
DR   RefSeq; WP_003093970.1; NZ_QZGE01000004.1.
DR   AlphaFoldDB; Q9HW51; -.
DR   SMR; Q9HW51; -.
DR   STRING; 287.DR97_1526; -.
DR   PaxDb; Q9HW51; -.
DR   PRIDE; Q9HW51; -.
DR   EnsemblBacteria; AAG07738; AAG07738; PA4350.
DR   GeneID; 881446; -.
DR   KEGG; pae:PA4350; -.
DR   PATRIC; fig|208964.12.peg.4555; -.
DR   PseudoCAP; PA4350; -.
DR   HOGENOM; CLU_058962_0_0_6; -.
DR   InParanoid; Q9HW51; -.
DR   OMA; YLRLGAW; -.
DR   PhylomeDB; Q9HW51; -.
DR   BioCyc; PAER208964:G1FZ6-4435-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0043810; F:ornithine-acyl [acyl carrier protein] N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..251
FT                   /note="L-ornithine N(alpha)-acyltransferase"
FT                   /id="PRO_0000452112"
SQ   SEQUENCE   251 AA;  28172 MW;  ABA800CCEFA91571 CRC64;
     MTQTAITREP VAGRRLKAER LNGARALREA QALRYRVFSA EFDAKLEGAE DGLDRDDYDR
     HCAHIGVRDL DSGALVATTR LLDHRAAERL GRFYSEEEFH LSGLDALHGP VLEIGRTCVA
     PEYRNGATIA VLWGELAEVL NEGGYRYLMG CASIPMRDGG MQAKAVMQRL RERYLCTDYL
     QAEPKNPLPP LDVPENLTAE LPPLLKAYMR LGAKICGEPC WDPDFQVADV FILLKRDELC
     PRYARHFKAA V