ID U7NKV4_9GAMM Unreviewed; 472 AA.
AC U7NKV4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=Q671_02905 {ECO:0000313|EMBL:ERS83907.1};
OS Halomonas sp. PBN3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS83907.1, ECO:0000313|Proteomes:UP000017115};
RN [1] {ECO:0000313|EMBL:ERS83907.1, ECO:0000313|Proteomes:UP000017115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBN3 {ECO:0000313|EMBL:ERS83907.1,
RC ECO:0000313|Proteomes:UP000017115};
RX PubMed=24356826;
RA Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA Kostka J.E.;
RT "Draft genome sequences for oil-degrading bacterial strains from beach
RT sands impacted by the deepwater horizon oil spill.";
RL Genome Announc. 1:e01015-13(2013).
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC 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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00190};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00190};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00190}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsA sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00190}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00190}.
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:ERS83907.1}.
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DR EMBL; AXCA01000185; ERS83907.1; -; Genomic_DNA.
DR RefSeq; WP_023006871.1; NZ_AXCA01000185.1.
DR AlphaFoldDB; U7NKV4; -.
DR PATRIC; fig|1397528.3.peg.2677; -.
DR eggNOG; COG1502; Bacteria.
DR Proteomes; UP000017115; 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; cd09155; PLDc_PaCLS_like_1; 1.
DR CDD; cd09161; PLDc_PaCLS_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR HAMAP; MF_00190; Cardiolipin_synth_ClsA; 1.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR030840; CL_synthase_A.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR NCBIfam; TIGR04265; bac_cardiolipin; 1.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
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|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00190};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00190};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00190}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00190}.
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT DOMAIN 210..237
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 385..412
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 215
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 217
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 390
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 392
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 397
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
SQ SEQUENCE 472 AA; 53717 MW; 2F24295EBAFC5780 CRC64;
MTSWLIGLAI FVIHLLGVVS AVLALMSSRT SQGAIAWILS LVTLPYVAVP AYWIFGRPRF
YGYVSARGER DTVLRRVLAR YRSRVDPYLA DIRDPDVRAV EQLAQMPMTS GNRAELLIDG
QATFDSIFAG LARAEEYALV QFFIVRNDAL GAELKRHLQQ AAERGVRVYF LYDEIGSHQL
NGGYLRDLAE AGIEVSAFRS SRGFRHRFQL NFRNHRKVVV VDGREGWVGG FNVGVEYLGE
HPRHGPWRDT HLKLTGPSVL GLQEAFWEDW HWATGEMITL DWVPRVTCEE CHKVVIVPSG
PADRQETASL LVQHAIHSAR ERFWVTSPYF VPDQGVQDAL RLAAMRGVDV RIMMPERPDH
LLVFLSAFSF LPDMLRAGVK VYRYQPGFLH QKVMLVDHEA ASVGTVNLDN RSFRLNFEIT
AFLPDRAFAA EVRVMLERDF ARCRRISLEE LTSRPLWRKL VSRAAYLLAP IQ
//
