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ID B2UI69_RALPJ Unreviewed; 477 AA.
AC B2UI69;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 08-MAY-2019, entry version 76.
DE RecName: Full=Cardiolipin synthase A {ECO:0000256|HAMAP-Rule:MF_00190};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_00190};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_00190};
GN Name=clsA {ECO:0000256|HAMAP-Rule:MF_00190};
GN OrderedLocusNames=Rpic_4171 {ECO:0000313|EMBL:ACD29270.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29270.1, ECO:0000313|Proteomes:UP000002566};
RN [1] {ECO:0000313|Proteomes:UP000002566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer
CC from one phosphatidylglycerol molecule to another to form
CC cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
CC {ECO:0000256|HAMAP-Rule:MF_00190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a
CC cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64716;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00190};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00190}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00190}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin
CC synthase subfamily. ClsA sub-subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00190}.
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DR EMBL; CP001069; ACD29270.1; -; Genomic_DNA.
DR RefSeq; WP_012430241.1; NC_010678.1.
DR STRING; 402626.Rpic_4171; -.
DR EnsemblBacteria; ACD29270; ACD29270; Rpic_4171.
DR GeneID; 6285595; -.
DR KEGG; rpi:Rpic_4171; -.
DR PATRIC; fig|402626.5.peg.417; -.
DR eggNOG; ENOG4105CQX; Bacteria.
DR eggNOG; COG1502; LUCA.
DR HOGENOM; HOG000077402; -.
DR KO; K06131; -.
DR OMA; GGHNVGD; -.
DR OrthoDB; 1881748at2; -.
DR Proteomes; UP000002566; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR HAMAP; MF_00190; Cardiolipin_synth_ClsA; 1.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR030840; CL_synthase_A.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00155; PLDc; 2.
DR TIGRFAMs; TIGR04265; bac_cardiolipin; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
DR PRODOM; B2UI69.
DR SWISS-2DPAGE; B2UI69.
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00190};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00190,
KW ECO:0000256|SAAS:SAAS00117509};
KW Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00190};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00190};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00190,
KW ECO:0000256|SAAS:SAAS00016851};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00190};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00190};
KW Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW Repeat {ECO:0000256|SAAS:SAAS00723978};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00190,
KW ECO:0000256|SAAS:SAAS00420582};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00190,
KW ECO:0000256|SAAS:SAAS00420576};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00190,
KW ECO:0000256|SAAS:SAAS00016984}.
FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}.
FT CHAIN 23 477 Cardiolipin synthase A. {ECO:0000256|SAM:
FT SignalP}.
FT /FTId=PRO_5002783529.
FT DOMAIN 216 243 PLD phosphodiesterase.
FT {ECO:0000259|PROSITE:PS50035}.
FT DOMAIN 390 417 PLD phosphodiesterase.
FT {ECO:0000259|PROSITE:PS50035}.
FT ACT_SITE 221 221 {ECO:0000256|HAMAP-Rule:MF_00190}.
FT ACT_SITE 223 223 {ECO:0000256|HAMAP-Rule:MF_00190}.
FT ACT_SITE 228 228 {ECO:0000256|HAMAP-Rule:MF_00190}.
FT ACT_SITE 395 395 {ECO:0000256|HAMAP-Rule:MF_00190}.
FT ACT_SITE 397 397 {ECO:0000256|HAMAP-Rule:MF_00190}.
FT ACT_SITE 402 402 {ECO:0000256|HAMAP-Rule:MF_00190}.
SQ SEQUENCE 477 AA; 53886 MW; DD1921C96EFED77E CRC64;
MLTNTTAFAA FLFLVHSVGV LAAMHAVLTV RTSQGAIAWA ISLVTLPEFT LIPYLIFGRS
TFAGYVDARR FHNARLREIT LSDDWRRLRD HESSVVAPQH TCMQALPRLT GTPCLARNRV
RLLVNGAETF EAIFAAIAQA RRVLIVQFFI VHDDTLGRRL AELLLDRARA GVRVYFLFDS
IGCHALPRRY VQRLIEGGVH AKPFSTHAGF VNRFQLNFRN HRKLVVVDGE RAYVGGHNVG
NEYMGEKPPL APWRDTHIEI VGAAVMDLQL TFAEDWYWAA REVPQLIVPE LRPEEDMVCQ
VVASGPADKQ ETCSLFFMEA IQSARKRLWI TSPYFIPDEA VFAALRLAVL RGVDVRILIP
SRPDHHMVFL ASTLYAYQAI RAGVKIYRYL PGFLHQKVVL IDDEAAAVGS ANLDNRSFRL
NFELMIMTAD SRFANDVAQM LEVDFAEAAR VGRDEYEHAH PLRRVIMHVA KLFAPIL
//
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