ID K8CD87_CROSK Unreviewed; 486 AA.
AC K8CD87;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=BN129_1416 {ECO:0000313|EMBL:CCK02848.1};
OS Cronobacter sakazakii 701.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1208663 {ECO:0000313|EMBL:CCK02848.1, ECO:0000313|Proteomes:UP000009355};
RN [1] {ECO:0000313|EMBL:CCK02848.1, ECO:0000313|Proteomes:UP000009355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=701 {ECO:0000313|EMBL:CCK02848.1,
RC ECO:0000313|Proteomes:UP000009355};
RX PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA McClelland M., Furtado M.R., Forsythe S.J.;
RT "Comparative analysis of genome sequences covering the seven cronobacter
RT species.";
RL PLoS ONE 7:e49455-e49455(2012).
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: 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:CCK02848.1}.
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DR EMBL; CALE01000616; CCK02848.1; -; Genomic_DNA.
DR AlphaFoldDB; K8CD87; -.
DR SMR; K8CD87; -.
DR PATRIC; fig|290339.8.peg.1374; -.
DR Proteomes; UP000009355; 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; cd09152; PLDc_EcCLS_like_1; 1.
DR CDD; cd09158; PLDc_EcCLS_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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT DOMAIN 219..246
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 399..426
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 226
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 404
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 406
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 411
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
SQ SEQUENCE 486 AA; 54709 MW; EE2786C2EE5174E0 CRC64;
MTTFYTVVSW LIILGYWLLI AGVTLRILMK RRAVPSAMAW LLVIYILPLV GIVAYLSVGE
LHLGKRRAER ARAMWPSTAK WLNDLKACKH IFAEENSAVA SALFQLCERR QGIAGVKGNQ
LQLLTSSDDV MQALIRDIQL ARHNIEMVFY IWQPGGMADQ VAESLMAAAR RGVHCRLMLD
SAGSVAFFRS PWAGMMRNAG IEVVEALKVN LMRVFLRRMD LRQHRKMIMI DNYIAYTGSM
NMVDPRYFKQ DAGVGQWVDL MARMEGPVAT AMGIVYSCDW EIETGKRLLP PPPDANIMPF
EQASGHTIHT IASGPGFPED LIHQALLTSV YAAREYLIMT TPYFVPSDDL LHAICTAAQR
GVDVSIILPR KNDSLLVGWA SRAFFSELLA AGVKIYQFEG GLLHTKSVLV DGELSLVGTV
NLDMRSLWLN FEITLVIDDA GFGADLAEVQ DDYISRSRLL DARLWVKRPF WQRVVERLFY
FFSPLL
//
