CLS2_BACAN
ID CLS2_BACAN Reviewed; 514 AA.
AC Q81TR2; Q6I1Z6; Q6KVT5;
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 2 {ECO:0000255|HAMAP-Rule:MF_01916};
DE Short=CL synthase 2 {ECO:0000255|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN Name=cls2; Synonyms=cls-2; OrderedLocusNames=BA_1204, GBAA_1204, BAS1112;
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; AAP25165.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30291.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53435.1; -; Genomic_DNA.
DR RefSeq; NP_843679.1; NC_003997.3.
DR RefSeq; WP_000799204.1; NZ_WXXJ01000044.1.
DR RefSeq; YP_027384.1; NC_005945.1.
DR AlphaFoldDB; Q81TR2; -.
DR SMR; Q81TR2; -.
DR IntAct; Q81TR2; 2.
DR STRING; 261594.GBAA_1204; -.
DR DNASU; 1087241; -.
DR EnsemblBacteria; AAP25165; AAP25165; BA_1204.
DR EnsemblBacteria; AAT30291; AAT30291; GBAA_1204.
DR GeneID; 59159014; -.
DR GeneID; 64200121; -.
DR KEGG; ban:BA_1204; -.
DR KEGG; bar:GBAA_1204; -.
DR KEGG; bat:BAS1112; -.
DR PATRIC; fig|198094.11.peg.1181; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_2_9; -.
DR OMA; HASRSYF; -.
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..514
FT /note="Cardiolipin synthase 2"
FT /id="PRO_0000201242"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 249..276
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 427..454
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 254
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 256
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 432
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 439
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ SEQUENCE 514 AA; 59501 MW; 68766F964B1897CC CRC64;
MKNTLKLIFF VLLLFALFVS LRMFIDVAFY SDVIGIKDVS ILGIISILFT VSAFLIGCVI
FLENRHPSKT LTWLIVLGIF PVFGFFAYLL FGQNFRRKRM FQKKALLDEQ AFLQYKGHED
YEERILRNHK HQELLFRLAD RLGALNISFQ TETRTLTNGD ETFQAILDGL KRAKHHIHME
YYIVRDDKLG TEIKDILIQK SKEGVVVRFL YDAVGSFKLS KSYIEELNDA GVEMIPFFPV
RFPILNDKIN YRNHRKIVII DGNEGFVGGL NIGDEYLGKD KYFGFWRDTH LYLRGEAVQS
LQLIFLQDWF YMTGEAVLAP EYLQAKAVEG EHWGGVQLVA GGPDNKWETI KHLYFAMIAS
ARKSIWIATP YFIPDDDILS ALKVAALAGI DVRLLMPSKP DKRTVFYASR SYFPELLDAG
VKIYEYEKGF LHSKVVIVDS DLASIGTANM DMRSFHLNFE VNAFLYDTDS IRKLVQDFKD
DLEESSEIHV DRFHKRRLHR RIVESTYRLL SPLL
