ID   OLSA_RHOCB              Reviewed;         276 AA.
AC   D5AQD5;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Lyso-ornithine lipid O-acyltransferase {ECO:0000305};
DE            EC=2.3.1.270 {ECO:0000250|UniProtKB:Q7APG1};
DE   AltName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000303|PubMed:17921310};
DE            Short=1-AGP acyltransferase {ECO:0000305};
DE            Short=1-AGPAT {ECO:0000303|PubMed:17921310};
DE            EC=2.3.1.n4 {ECO:0000269|PubMed:17921310};
GN   Name=olsA {ECO:0000303|PubMed:16856942};
GN   OrderedLocusNames=RCAP_rcc02997 {ECO:0000312|EMBL:ADE86724.1};
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [2]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MT1131;
RX   PubMed=16856942; DOI=10.1111/j.1365-2958.2006.05253.x;
RA   Aygun-Sunar S., Mandaci S., Koch H.G., Murray I.V., Goldfine H., Daldal F.;
RT   "Ornithine lipid is required for optimal steady-state amounts of c-type
RT   cytochromes in Rhodobacter capsulatus.";
RL   Mol. Microbiol. 61:418-435(2006).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=MT1131;
RX   PubMed=17921310; DOI=10.1128/jb.01121-07;
RA   Aygun-Sunar S., Bilaloglu R., Goldfine H., Daldal F.;
RT   "Rhodobacter capsulatus OlsA is a bifunctional enzyme active in both
RT   ornithine lipid and phosphatidic acid biosynthesis.";
RL   J. Bacteriol. 189:8564-8574(2007).
CC   -!- FUNCTION: Catalyzes the second step in the formation of ornithine
CC       lipids, which are phosphorus-free membrane lipids (Probable). Uses
CC       acyl-acyl carrier protein (acyl-AcpP) as an acyl donor and converts
CC       lyso-ornithine lipid (LOL) into ornithine lipid (OL) (By similarity).
CC       It can also act as an alternate acyl-sn-glycerol-3-phosphate
CC       acyltransferase (AGPAT) to ensure glycerophospholipid production
CC       (PubMed:17921310). {ECO:0000250|UniProtKB:Q7APG1,
CC       ECO:0000269|PubMed:17921310, ECO:0000305|PubMed:16856942}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-
CC         diacyl-sn-glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42296,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57970,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC         EC=2.3.1.n4; Evidence={ECO:0000269|PubMed:17921310};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000269|PubMed:16856942}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000269|PubMed:17921310}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Mutant lacking this gene is unable to produce
CC       ornithine lipids. {ECO:0000269|PubMed:16856942}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. OlsA subfamily. {ECO:0000305}.
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DR   EMBL; CP001312; ADE86724.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5AQD5; -.
DR   SMR; D5AQD5; -.
DR   STRING; 272942.RCAP_rcc02997; -.
DR   EnsemblBacteria; ADE86724; ADE86724; RCAP_rcc02997.
DR   KEGG; rcp:RCAP_rcc02997; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_0_1_5; -.
DR   OMA; DPRFYGW; -.
DR   Proteomes; UP000002361; 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:0008654; P:phospholipid biosynthetic 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   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..276
FT                   /note="Lyso-ornithine lipid O-acyltransferase"
FT                   /id="PRO_0000452118"
FT   TRANSMEM        25..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   276 AA;  30719 MW;  DF626AD9FA3EA5DB CRC64;
     MTRPIWMGDE PPPDRPPTLA GRGRLALRGG AMALVLMAGL TLHLAVRLIE RPLHGGHRPW
     TPAITPVVCR ICVAILGLRY SVRGRPMQHI GAVVANHTGW LDIFTLNACQ RLYFVSKDEV
     ADWPFIGWLA RATGTVFIRR DPREAKAQQA LLEDRIRDGH HLLFFPEGTS TDGLQVLPFK
     TTLFAAFYTH GLDKVMQIQP VTVNYTAPEG EDPRFYGWWR DMPFATHLAK VLSVARQGAA
     EVVFHPPLDV SDFPSRKDLA AACEAAVRSG MGQRSR