CLSA_ECO57
ID CLSA_ECO57 Reviewed; 486 AA.
AC Q8XCC6;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cardiolipin synthase A {ECO:0000255|HAMAP-Rule:MF_00190};
DE Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_00190};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_00190};
GN Name=clsA {ECO:0000255|HAMAP-Rule:MF_00190}; Synonyms=cls;
GN OrderedLocusNames=Z2026, ECs1749;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00190};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00190}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00190}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsA sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_00190}.
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DR EMBL; AE005174; AAG56104.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35172.1; -; Genomic_DNA.
DR PIR; D85705; D85705.
DR PIR; E90847; E90847.
DR RefSeq; NP_309776.1; NC_002695.1.
DR RefSeq; WP_000214510.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XCC6; -.
DR SMR; Q8XCC6; -.
DR STRING; 155864.EDL933_1953; -.
DR EnsemblBacteria; AAG56104; AAG56104; Z2026.
DR EnsemblBacteria; BAB35172; BAB35172; ECs_1749.
DR GeneID; 913102; -.
DR KEGG; ece:Z2026; -.
DR KEGG; ecs:ECs_1749; -.
DR PATRIC; fig|386585.9.peg.1851; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_0_6; -.
DR OMA; TRFILDW; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR TIGRFAMs; TIGR04265; bac_cardiolipin; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..486
FT /note="Cardiolipin synthase A"
FT /id="PRO_0000201255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 219..246
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 399..426
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 224
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 226
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 231
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 404
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 406
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 411
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ SEQUENCE 486 AA; 54789 MW; 3D6B607782A22C1C CRC64;
MTTVYTLVSW LAILGYWLLI AGVTLRILMK RRAVPSAMAW LLIIYILPLV GIIAYLAVGE
LHLGKRRAER ARAMWPSTAK WLNDLKACKH IFAEENSSVA APLFKLCERR QGIAGVKGNQ
LQLMTESDDV MQALIRDIQL ARHNIEMVFY IWQPGGMADQ VAESLMAAAR RGIHCRLMLD
SAGSVAFFHS PWPELMRNAG IEVVEALKVN LMRVFLRRMD LRQHRKMIMI DNYIAYTGSM
NMVDPRYFKQ DAGVGQWIDL MARMEGPIAT AMGIIYSCDW EIETGKRILP PPPDVNIMPF
EQASGHTIHT IASGPGFPED LIHQALLTAA YSAREYLIMT TPYFVPSDDL LHAICTAAQR
GVDVSIILPR KNDSMLVGWA SRAFFTELLA AGVKVYQFEG GLLHTKSVLV DGELSLVGTV
NLDMRSLWLN FEITLAIDDK GFGADLAAVQ DDYISRSRLL DARLWLKRPL WQRVAERLFY
FFSPLL
