(data stored in SCRATCH zone)

SWISSPROT: B2UI69_RALPJ

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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
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
//

If you have problems or comments...

PBIL Back to PBIL home page