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Protein

Cardiolipin synthase B

Gene

clsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Can also catalyze phosphatidyl group transfer to water to form phosphatidate.UniRule annotation2 Publications

Catalytic activityi

2 Phosphatidylglycerol = diphosphatidylglycerol + glycerol.UniRule annotation

Enzyme regulationi

Activated by phosphate. Inhibited by cardiolipin and phosphatidate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei113 – 1131UniRule annotation
Active sitei115 – 1151UniRule annotation
Active sitei120 – 1201UniRule annotation
Active sitei290 – 2901UniRule annotation
Active sitei292 – 2921UniRule annotation
Active sitei297 – 2971UniRule annotation

GO - Molecular functioni

  • cardiolipin synthase activity Source: EcoCyc
  • phospholipase D activity Source: EcoliWiki

GO - Biological processi

  • cardiolipin biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:G6406-MONOMER.
ECOL316407:JW0772-MONOMER.
MetaCyc:G6406-MONOMER.
BRENDAi2.7.8.B10. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Cardiolipin synthase BUniRule annotation (EC:2.7.8.-UniRule annotation)
Short name:
CL synthaseUniRule annotation
Gene namesi
Name:clsBUniRule annotation
Synonyms:ybhO
Ordered Locus Names:b0789, JW0772
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13671. clsB.

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  • membrane Source: EcoCyc
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Triple deletion of clsA, clsB and clsC results in a complete lack of cardiolipin, regardless of growth phase or growth conditions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413Cardiolipin synthase BPRO_0000201283Add
BLAST

Proteomic databases

PaxDbiP0AA84.
PRIDEiP0AA84.

Interactioni

Protein-protein interaction databases

BioGridi4259959. 389 interactions.
IntActiP0AA84. 5 interactions.
STRINGi511145.b0789.

Structurei

3D structure databases

ProteinModelPortaliP0AA84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 13528PLD phosphodiesterase 1UniRule annotationAdd
BLAST
Domaini285 – 31228PLD phosphodiesterase 2UniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsB sub-subfamily.UniRule annotation
Contains 2 PLD phosphodiesterase domains.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105DZQ. Bacteria.
COG1502. LUCA.
HOGENOMiHOG000264393.
InParanoidiP0AA84.
KOiK06131.
OMAiTHRKILI.
OrthoDBiEOG6Q2ST0.
PhylomeDBiP0AA84.

Family and domain databases

HAMAPiMF_01917. Cardiolipin_synth_ClsB.
InterProiIPR030872. Cardiolipin_synth_ClsB.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamiPF13091. PLDc_2. 2 hits.
[Graphical view]
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AA84-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCSWREGNK IQLLENGEQY YPAVFKAIGE AQERIILETF IWFEDDVGKQ
60 70 80 90 100
LHAALLAAAQ RGVKAEVLLD GYGSPDLSDE FVNELTAAGV VFRYYDPRPR
110 120 130 140 150
LFGMRTNVFR RMHRKIVVID ARIAFIGGLN YSAEHMSSYG PEAKQDYAVR
160 170 180 190 200
LEGPIVEDIL QFELENLPGQ SAARRWWRRH HKAEENRQPG EAQVLLVWRD
210 220 230 240 250
NEEHRDDIER HYLKMLTQAR REVIIANAYF FPGYRFLHAL RKAARRGVRI
260 270 280 290 300
KLIIQGEPDM PIVRVGARLL YNYLVKGGVQ VFEYRRRPLH GKVALMDDHW
310 320 330 340 350
ATVGSSNLDP LSLSLNLEAN VIIHDRHFNQ TLRDNLNGII AADCQQVDET
360 370 380 390 400
MLPKRTWWNL TKSVLAFHFL RHFPALVGWL PAHTPRLAQV DPPAQPTMET
410
QDRVETENTG VKP
Length:413
Mass (Da):47,634
Last modified:September 13, 2005 - v1
Checksum:i74998B2A1AD24A11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73876.1.
AP009048 Genomic DNA. Translation: BAA35448.1.
PIRiE64815.
RefSeqiNP_415310.1. NC_000913.3.
WP_000650337.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73876; AAC73876; b0789.
BAA35448; BAA35448; BAA35448.
GeneIDi945409.
KEGGiecj:JW0772.
eco:b0789.
PATRICi32116779. VBIEscCol129921_0815.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73876.1.
AP009048 Genomic DNA. Translation: BAA35448.1.
PIRiE64815.
RefSeqiNP_415310.1. NC_000913.3.
WP_000650337.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AA84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259959. 389 interactions.
IntActiP0AA84. 5 interactions.
STRINGi511145.b0789.

Proteomic databases

PaxDbiP0AA84.
PRIDEiP0AA84.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73876; AAC73876; b0789.
BAA35448; BAA35448; BAA35448.
GeneIDi945409.
KEGGiecj:JW0772.
eco:b0789.
PATRICi32116779. VBIEscCol129921_0815.

Organism-specific databases

EchoBASEiEB3435.
EcoGeneiEG13671. clsB.

Phylogenomic databases

eggNOGiENOG4105DZQ. Bacteria.
COG1502. LUCA.
HOGENOMiHOG000264393.
InParanoidiP0AA84.
KOiK06131.
OMAiTHRKILI.
OrthoDBiEOG6Q2ST0.
PhylomeDBiP0AA84.

Enzyme and pathway databases

BioCyciEcoCyc:G6406-MONOMER.
ECOL316407:JW0772-MONOMER.
MetaCyc:G6406-MONOMER.
BRENDAi2.7.8.B10. 2026.

Miscellaneous databases

PROiP0AA84.

Family and domain databases

HAMAPiMF_01917. Cardiolipin_synth_ClsB.
InterProiIPR030872. Cardiolipin_synth_ClsB.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamiPF13091. PLDc_2. 2 hits.
[Graphical view]
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "A second Escherichia coli protein with CL synthase activity."
    Guo D., Tropp B.E.
    Biochim. Biophys. Acta 1483:263-274(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CL SYNTHASE, ENZYME REGULATION, SUBCELLULAR LOCATION.
    Strain: ATCC 33694 / HB101.
  5. "Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates."
    Tan B.K., Bogdanov M., Zhao J., Dowhan W., Raetz C.R., Guan Z.
    Proc. Natl. Acad. Sci. U.S.A. 109:16504-16509(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, GENE NAME.

Entry informationi

Entry nameiCLSB_ECOLI
AccessioniPrimary (citable) accession number: P0AA84
Secondary accession number(s): P75771
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: April 13, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

All three cardiolipin synthases (ClsA, ClsB and ClsC) contribute to CL synthesis in stationary phase. Only ClsA contributes to synthesis during logarithmic growth phase (PubMed:22988102).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.