CLS1_BACAN
ID CLS1_BACAN Reviewed; 509 AA.
AC Q81V75; Q6I3G1; Q6KX75;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Cardiolipin synthase 1 {ECO:0000255|HAMAP-Rule:MF_01916};
DE Short=CL synthase 1 {ECO:0000255|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN Name=cls1; Synonyms=cls-1; OrderedLocusNames=BA_0625, GBAA_0625, BAS0592;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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_01916}.
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_01916};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01916};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01916}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01916}.
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DR EMBL; AE016879; AAP24642.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29728.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52920.1; -; Genomic_DNA.
DR RefSeq; NP_843156.1; NC_003997.3.
DR RefSeq; WP_000742930.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_026869.1; NC_005945.1.
DR AlphaFoldDB; Q81V75; -.
DR SMR; Q81V75; -.
DR STRING; 261594.GBAA_0625; -.
DR DNASU; 1088023; -.
DR EnsemblBacteria; AAP24642; AAP24642; BA_0625.
DR EnsemblBacteria; AAT29728; AAT29728; GBAA_0625.
DR GeneID; 45020686; -.
DR KEGG; ban:BA_0625; -.
DR KEGG; bar:GBAA_0625; -.
DR KEGG; bat:BAS0592; -.
DR PATRIC; fig|198094.11.peg.623; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_2_9; -.
DR OMA; YAPWVDI; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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_01916; Cardiolipin_synth_Cls; 1.
DR InterPro; IPR030874; Cardiolipin_synth_Firmi.
DR InterPro; IPR022924; Cardiolipin_synthase.
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 membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Cardiolipin synthase 1"
FT /id="PRO_0000201241"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 238..265
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 422..449
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 245
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 427
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 429
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ SEQUENCE 509 AA; 58107 MW; 54AFD680C2A095FA CRC64;
MKKPIIQLLL IFTIVSIVPF LLNTSYISLY TFVGVLWSIT IVGISFVIFI ENRSPQSTLA
WFLVLALLPV VGVLLYSIFG RSRWRRKKHL HRSEEQRKLF REILEGRRLE LSLKVPLSER
SVHLTEVVQK FGGGPAADRT TTKLLTNGDQ TFSEILQAIE QAKHHIHIQY YIYKSDEIGT
KVRDALIKKA KDGVIVRFLY DGLGSNTLRR RFLQPMKEAG IEIVEFDPIF SAWLLETVNY
RNHRKIVIVD GEIGFTGGLN VGDEYLGRSK KFPVWRDSHL KVEGKALYKL QAIFLEDWLY
ASSGLNTYSW DPFMNRQYFP GKEISNAEGA VQIVASGPSS DDKSIRNTLL AVMGSAKKSI
WIATPYFIPD QETLTLLRLS AISGIDVRIL YPGKSDSIIS DQASQSYFTP LLKAGASIYS
YKDGFMHAKI LLVDDKIATI GTANMDVRSF ELNYEIISVL YESETVHDIK RDFEDDFKHS
TEIKWNAFQK RSIKKRILES FMRLISPLL
