CLSB_ECOLI
ID CLSB_ECOLI Reviewed; 413 AA.
AC P0AA84; P75771;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cardiolipin synthase B {ECO:0000255|HAMAP-Rule:MF_01917};
DE Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_01917};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01917, ECO:0000269|PubMed:10634942};
GN Name=clsB {ECO:0000255|HAMAP-Rule:MF_01917, ECO:0000303|PubMed:22988102};
GN Synonyms=ybhO; OrderedLocusNames=b0789, JW0772;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A CL SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33694 / HB101;
RX PubMed=10634942; DOI=10.1016/s1388-1981(99)00193-6;
RA Guo D., Tropp B.E.;
RT "A second Escherichia coli protein with CL synthase activity.";
RL Biochim. Biophys. Acta 1483:263-274(2000).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RX PubMed=22988102; DOI=10.1073/pnas.1212797109;
RA Tan B.K., Bogdanov M., Zhao J., Dowhan W., Raetz C.R., Guan Z.;
RT "Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and
RT phosphatidylglycerol as substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16504-16509(2012).
CC -!- FUNCTION: Catalyzes the phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. Can also catalyze phosphatidyl
CC group transfer to water to form phosphatidate. {ECO:0000255|HAMAP-
CC Rule:MF_01917, ECO:0000269|PubMed:10634942,
CC ECO:0000269|PubMed:22988102}.
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_01917, ECO:0000269|PubMed:10634942};
CC -!- ACTIVITY REGULATION: Activated by phosphate. Inhibited by cardiolipin
CC and phosphatidate. {ECO:0000269|PubMed:10634942}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10634942};
CC Peripheral membrane protein {ECO:0000305|PubMed:10634942}.
CC -!- DISRUPTION PHENOTYPE: Triple deletion of clsA, clsB and clsC results in
CC a complete lack of cardiolipin, regardless of growth phase or growth
CC conditions. {ECO:0000269|PubMed:22988102}.
CC -!- MISCELLANEOUS: All three cardiolipin synthases (ClsA, ClsB and ClsC)
CC contribute to CL synthesis in stationary phase. Only ClsA contributes
CC to synthesis during logarithmic growth phase.
CC {ECO:0000305|PubMed:22988102}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsB sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_01917}.
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DR EMBL; U00096; AAC73876.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35448.1; -; Genomic_DNA.
DR PIR; E64815; E64815.
DR RefSeq; NP_415310.1; NC_000913.3.
DR RefSeq; WP_000650337.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P0AA84; -.
DR SMR; P0AA84; -.
DR BioGRID; 4259959; 389.
DR IntAct; P0AA84; 5.
DR STRING; 511145.b0789; -.
DR jPOST; P0AA84; -.
DR PaxDb; P0AA84; -.
DR PRIDE; P0AA84; -.
DR EnsemblBacteria; AAC73876; AAC73876; b0789.
DR EnsemblBacteria; BAA35448; BAA35448; BAA35448.
DR GeneID; 66670939; -.
DR GeneID; 945409; -.
DR KEGG; ecj:JW0772; -.
DR KEGG; eco:b0789; -.
DR PATRIC; fig|1411691.4.peg.1489; -.
DR EchoBASE; EB3435; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_0_0_6; -.
DR InParanoid; P0AA84; -.
DR OMA; EYCQRPL; -.
DR PhylomeDB; P0AA84; -.
DR BioCyc; EcoCyc:G6406-MON; -.
DR BioCyc; MetaCyc:G6406-MON; -.
DR BRENDA; 2.7.8.B10; 2026.
DR PRO; PR:P0AA84; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IDA:EcoCyc.
DR GO; GO:0004630; F:phospholipase D activity; IDA:EcoliWiki.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:EcoCyc.
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 Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..413
FT /note="Cardiolipin synthase B"
FT /id="PRO_0000201283"
FT DOMAIN 108..135
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT DOMAIN 285..312
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT REGION 390..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT ACT_SITE 115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT ACT_SITE 120
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT ACT_SITE 290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT ACT_SITE 292
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT ACT_SITE 297
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
SQ SEQUENCE 413 AA; 47634 MW; 74998B2A1AD24A11 CRC64;
MKCSWREGNK IQLLENGEQY YPAVFKAIGE AQERIILETF IWFEDDVGKQ LHAALLAAAQ
RGVKAEVLLD GYGSPDLSDE FVNELTAAGV VFRYYDPRPR LFGMRTNVFR RMHRKIVVID
ARIAFIGGLN YSAEHMSSYG PEAKQDYAVR LEGPIVEDIL QFELENLPGQ SAARRWWRRH
HKAEENRQPG EAQVLLVWRD NEEHRDDIER HYLKMLTQAR REVIIANAYF FPGYRFLHAL
RKAARRGVRI KLIIQGEPDM PIVRVGARLL YNYLVKGGVQ VFEYRRRPLH GKVALMDDHW
ATVGSSNLDP LSLSLNLEAN VIIHDRHFNQ TLRDNLNGII AADCQQVDET MLPKRTWWNL
TKSVLAFHFL RHFPALVGWL PAHTPRLAQV DPPAQPTMET QDRVETENTG VKP
