CLSA_BACSU
ID CLSA_BACSU Reviewed; 482 AA.
AC P71040;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Major cardiolipin synthase ClsA;
DE Short=CL synthase 2 {ECO:0000255|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN Name=clsA; Synonyms=ywnE; OrderedLocusNames=BSU36590;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9150240; DOI=10.1128/jb.179.10.3371-3373.1997;
RA Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H.;
RT "The Bacillus subtilis ureABC operon.";
RL J. Bacteriol. 179:3371-3373(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION IN THE CARDIOLIPIN BIOSYNTHESIS, DISRUPTION PHENOTYPE, AND
RP NOMENCLATURE.
RX PubMed=14973018; DOI=10.1128/jb.186.5.1475-1483.2004;
RA Kawai F., Shoda M., Harashima R., Sadaie Y., Hara H., Matsumoto K.;
RT "Cardiolipin domains in Bacillus subtilis marburg membranes.";
RL J. Bacteriol. 186:1475-1483(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15743965; DOI=10.1128/jb.187.6.2163-2174.2005;
RA Nishibori A., Kusaka J., Hara H., Umeda M., Matsumoto K.;
RT "Phosphatidylethanolamine domains and localization of phospholipid
RT synthases in Bacillus subtilis membranes.";
RL J. Bacteriol. 187:2163-2174(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
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, ECO:0000269|PubMed:14973018}.
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:0000305|PubMed:15743965};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15743965}.
CC Note=Localized in the septal membrane. Localization depnds on FtsZ.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a lack of
CC cardiolipin (PubMed:14973018). Cells appear normal, no effect on
CC flotillin cluster numbers or size (PubMed:27362352).
CC {ECO:0000269|PubMed:14973018, ECO:0000269|PubMed:27362352}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01916}.
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DR EMBL; Y08559; CAA69864.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15676.1; -; Genomic_DNA.
DR PIR; G70063; G70063.
DR RefSeq; NP_391540.1; NC_000964.3.
DR RefSeq; WP_003243311.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P71040; -.
DR SMR; P71040; -.
DR STRING; 224308.BSU36590; -.
DR PaxDb; P71040; -.
DR DNASU; 936957; -.
DR EnsemblBacteria; CAB15676; CAB15676; BSU_36590.
DR GeneID; 936957; -.
DR KEGG; bsu:BSU36590; -.
DR PATRIC; fig|224308.179.peg.3960; -.
DR eggNOG; COG1502; Bacteria.
DR InParanoid; P71040; -.
DR OMA; TRFILDW; -.
DR PhylomeDB; P71040; -.
DR BioCyc; BSUB:BSU36590-MON; -.
DR BRENDA; 2.7.8.41; 658.
DR Proteomes; UP000001570; 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; IMP:UniProtKB.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0043934; P:sporulation; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
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; IPR000515; MetI-like.
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 1: Evidence at protein level;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..482
FT /note="Major cardiolipin synthase ClsA"
FT /id="PRO_0000201248"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 217..244
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 395..422
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 222
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 224
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 229
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 400
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 402
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 407
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ SEQUENCE 482 AA; 55866 MW; 8231FC35DB3CAC63 CRC64;
MSISSILLSL FFILNILLAI IVIFKERRDA SASWAWLLVL FFIPVLGFIL YLLFGHNLRR
KHLFQWEDRK KIGIERLLKH QLEDLETKQF QFNNRATFDN KDLIYMLIMN NHAVFTEDNS
VDVITDGRDK FQRLLSDISK AKDHIHLQYY IYKGDELGKK LRDALIQKAK EGVQVRVLYD
ELGSRTLRKK FFKELREAGG HVEVFFPSKL RPINLRLNYR NHRKLVIIDG MTGYVGGFNV
GDEYLGLNPK FGYWRDTHIR LQGTAVHAIQ TRFILDWNQA SHHHTLTYIP NHFPDYGPKG
NVGMQIVTSG PDSEWEQIKN GYIKMISNAK RSILIQTPYF IPDASLLDAL RIACLSGIDV
NIMIPNKPDH AFVYWATLSY IGDLLKAGAT VYIYDNGFIH AKTIVVDDEI ASVGTANIDV
RSFRLNFEVN AFIYDITIAK KLVSTFKEDL LVSRKFTYEE YLQRPLWIRI KESVSRLLSP
IL
