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Database: UniProt
Entry: I8I5C8_9GAMM
LinkDB: I8I5C8_9GAMM
Original site: I8I5C8_9GAMM 
ID   I8I5C8_9GAMM            Unreviewed;       425 AA.
AC   I8I5C8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Cardiolipin synthase B {ECO:0000256|HAMAP-Rule:MF_01917};
DE            Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01917};
DE            EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01917};
GN   Name=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN   ORFNames=WQQ_17330 {ECO:0000313|EMBL:EIT71596.1};
OS   Hydrocarboniphaga effusa AP103.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Hydrocarboniphaga.
OX   NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT71596.1, ECO:0000313|Proteomes:UP000003704};
RN   [1] {ECO:0000313|EMBL:EIT71596.1, ECO:0000313|Proteomes:UP000003704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP103 {ECO:0000313|EMBL:EIT71596.1,
RC   ECO:0000313|Proteomes:UP000003704};
RX   PubMed=22933753; DOI=10.1128/JB.01017-12;
RA   Chang H.K., Zylstra G.J., Chae J.C.;
RT   "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT   AP103T (ATCC BAA-332T).";
RL   J. Bacteriol. 194:5120-5120(2012).
CC   -!- FUNCTION: Catalyzes the phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC       Rule:MF_01917}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01917};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01917};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01917}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. ClsB sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01917}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIT71596.1}.
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DR   EMBL; AKGD01000001; EIT71596.1; -; Genomic_DNA.
DR   RefSeq; WP_007184682.1; NZ_AKGD01000001.1.
DR   AlphaFoldDB; I8I5C8; -.
DR   STRING; 1172194.WQQ_17330; -.
DR   PATRIC; fig|1172194.4.peg.1674; -.
DR   OrthoDB; 9762009at2; -.
DR   Proteomes; UP000003704; Unassembled WGS sequence.
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   CDD; cd09110; PLDc_CLS_1; 1.
DR   CDD; cd09159; PLDc_ybhO_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   HAMAP; MF_01917; Cardiolipin_synth_ClsB; 1.
DR   InterPro; IPR030872; Cardiolipin_synth_ClsB.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR   PANTHER; PTHR21248:SF23; CARDIOLIPIN SYNTHASE B; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003704};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   DOMAIN          112..139
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          296..323
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          395..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ   SEQUENCE   425 AA;  49103 MW;  B65A14B17FE6E798 CRC64;
     MKDDRRHPWR AGNRVQLLEN GEAYYPRVLE IVNAAEKEIF VETFILFDDP VGKPFQQALI
     AAARRGCRVE LTVDGYGSAN LTPEFIGEMT SVGIQFHVYR PQPKVMGMRT NLFRRLHRKL
     IVVDGRIAFC GGINIAFDHV ADFGPTSKQD YAVEVEGPIV RDIHRFVELS VAKSEAKQNR
     LKRWWQRRKQ AIPEPEHASV GSVNAMFVIR DNERHHDDIE RQYRLAIKSA RSRIVIANAY
     FFPGWRLLRN LRDAARRGVD VTLILQGKPD MWYVKWVAEN LYHYLMKAGV RIYEYCERPL
     HAKVAVIDDH WATVGSSNLD PLSLYLNLES NLVFRDAAFN AHLASRLRHL MQQCCREVQW
     DSIPHRDIRR QLFVFITYHL GRRFPAWAGW RPAHAQKQGI AAPDSRPPDD QREAPGSLQA
     QSAKH
//
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