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Protein

Major cardiolipin synthase ClsA

Gene

clsA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.UniRule annotation1 Publication

Catalytic activityi

2 Phosphatidylglycerol = diphosphatidylglycerol + glycerol.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei222 – 2221UniRule annotation
Active sitei224 – 2241UniRule annotation
Active sitei229 – 2291UniRule annotation
Active sitei400 – 4001UniRule annotation
Active sitei402 – 4021UniRule annotation
Active sitei407 – 4071UniRule annotation

GO - Molecular functioni

  • cardiolipin synthase activity Source: UniProtKB

GO - Biological processi

  • cardiolipin biosynthetic process Source: UniProtKB
  • sporulation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU36590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Major cardiolipin synthase ClsA (EC:2.7.8.-UniRule annotation)
Short name:
CL synthase 2UniRule annotation
Gene namesi
Name:clsA
Synonyms:ywnE
Ordered Locus Names:BSU36590
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei3 – 2321HelicalUniRule annotationAdd
BLAST
Transmembranei34 – 5421HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show a lack of cardiolipin.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Major cardiolipin synthase ClsAPRO_0000201248Add
BLAST

Proteomic databases

PaxDbiP71040.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019781.

Structurei

3D structure databases

ProteinModelPortaliP71040.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini217 – 24428PLD phosphodiesterase 1UniRule annotationAdd
BLAST
Domaini395 – 42228PLD phosphodiesterase 2UniRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CQX. Bacteria.
COG1502. LUCA.
HOGENOMiHOG000077402.
InParanoidiP71040.
KOiK06131.
OMAiYDITIAK.
OrthoDBiEOG6Q2ST0.
PhylomeDBiP71040.

Family and domain databases

HAMAPiMF_01916. Cardiolipin_synth_Cls.
InterProiIPR030874. Cardiolipin_synth_Firmi.
IPR022924. Cardiolipin_synthase.
IPR027379. CLS_N.
IPR000515. MetI-like.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamiPF13091. PLDc_2. 2 hits.
PF13396. PLDc_N. 1 hit.
[Graphical view]
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
TIGRFAMsiTIGR04265. bac_cardiolipin. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P71040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSISSILLSL FFILNILLAI IVIFKERRDA SASWAWLLVL FFIPVLGFIL
60 70 80 90 100
YLLFGHNLRR KHLFQWEDRK KIGIERLLKH QLEDLETKQF QFNNRATFDN
110 120 130 140 150
KDLIYMLIMN NHAVFTEDNS VDVITDGRDK FQRLLSDISK AKDHIHLQYY
160 170 180 190 200
IYKGDELGKK LRDALIQKAK EGVQVRVLYD ELGSRTLRKK FFKELREAGG
210 220 230 240 250
HVEVFFPSKL RPINLRLNYR NHRKLVIIDG MTGYVGGFNV GDEYLGLNPK
260 270 280 290 300
FGYWRDTHIR LQGTAVHAIQ TRFILDWNQA SHHHTLTYIP NHFPDYGPKG
310 320 330 340 350
NVGMQIVTSG PDSEWEQIKN GYIKMISNAK RSILIQTPYF IPDASLLDAL
360 370 380 390 400
RIACLSGIDV NIMIPNKPDH AFVYWATLSY IGDLLKAGAT VYIYDNGFIH
410 420 430 440 450
AKTIVVDDEI ASVGTANIDV RSFRLNFEVN AFIYDITIAK KLVSTFKEDL
460 470 480
LVSRKFTYEE YLQRPLWIRI KESVSRLLSP IL
Length:482
Mass (Da):55,866
Last modified:July 1, 1997 - v2
Checksum:i8231FC35DB3CAC63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08559 Genomic DNA. Translation: CAA69864.1.
AL009126 Genomic DNA. Translation: CAB15676.1.
PIRiG70063.
RefSeqiNP_391540.1. NC_000964.3.
WP_003243311.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15676; CAB15676; BSU36590.
GeneIDi936957.
KEGGibsu:BSU36590.
PATRICi18979346. VBIBacSub10457_3835.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08559 Genomic DNA. Translation: CAA69864.1.
AL009126 Genomic DNA. Translation: CAB15676.1.
PIRiG70063.
RefSeqiNP_391540.1. NC_000964.3.
WP_003243311.1. NZ_JNCM01000034.1.

3D structure databases

ProteinModelPortaliP71040.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019781.

Proteomic databases

PaxDbiP71040.

Protocols and materials databases

DNASUi936957.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15676; CAB15676; BSU36590.
GeneIDi936957.
KEGGibsu:BSU36590.
PATRICi18979346. VBIBacSub10457_3835.

Phylogenomic databases

eggNOGiENOG4105CQX. Bacteria.
COG1502. LUCA.
HOGENOMiHOG000077402.
InParanoidiP71040.
KOiK06131.
OMAiYDITIAK.
OrthoDBiEOG6Q2ST0.
PhylomeDBiP71040.

Enzyme and pathway databases

BioCyciBSUB:BSU36590-MONOMER.

Family and domain databases

HAMAPiMF_01916. Cardiolipin_synth_Cls.
InterProiIPR030874. Cardiolipin_synth_Firmi.
IPR022924. Cardiolipin_synthase.
IPR027379. CLS_N.
IPR000515. MetI-like.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamiPF13091. PLDc_2. 2 hits.
PF13396. PLDc_N. 1 hit.
[Graphical view]
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
TIGRFAMsiTIGR04265. bac_cardiolipin. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Bacillus subtilis ureABC operon."
    Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H.
    J. Bacteriol. 179:3371-3373(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Cardiolipin domains in Bacillus subtilis marburg membranes."
    Kawai F., Shoda M., Harashima R., Sadaie Y., Hara H., Matsumoto K.
    J. Bacteriol. 186:1475-1483(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE CARDIOLIPIN BIOSYNTHESIS, DISRUPTION PHENOTYPE, NOMENCLATURE.
  4. "Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes."
    Nishibori A., Kusaka J., Hara H., Umeda M., Matsumoto K.
    J. Bacteriol. 187:2163-2174(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCLSA_BACSU
AccessioniPrimary (citable) accession number: P71040
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: July 6, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.