CLS1_BACSU
ID CLS1_BACSU Reviewed; 500 AA.
AC P45860;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable cardiolipin synthase YwiE;
DE Short=CL synthase 1 {ECO:0000255|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN Name=ywiE; OrderedLocusNames=BSU37240;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8846791;
RA Cruz Ramos H., Boursier L., Moszer I., Kunst F., Danchin A., Glaser P.;
RT "Anaerobic transcription activation in Bacillus subtilis: identification of
RT distinct FNR-dependent and -independent regulatory mechanisms.";
RL EMBO J. 14:5984-5994(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
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 [4]
RP PUTATIVE FUNCTION, AND INDUCTION.
RX PubMed=11717291; DOI=10.1128/jb.183.24.7318-7328.2001;
RA Helmann J.D., Wu M.F., Kobel P.A., Gamo F.J., Wilson M., Morshedi M.M.,
RA Navre M., Paddon C.;
RT "Global transcriptional response of Bacillus subtilis to heat shock.";
RL J. Bacteriol. 183:7318-7328(2001).
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol (By similarity). May have a role
CC in the heat shock response since the level of the transcript of ywiE
CC increases after a heat shock. {ECO:0000255|HAMAP-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 -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:11717291}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01916}.
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DR EMBL; Z49884; CAA90049.1; -; Genomic_DNA.
DR EMBL; Z49782; CAA89861.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15752.1; -; Genomic_DNA.
DR PIR; S60089; S60089.
DR RefSeq; NP_391605.1; NC_000964.3.
DR RefSeq; WP_003242612.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P45860; -.
DR SMR; P45860; -.
DR IntAct; P45860; 7.
DR STRING; 224308.BSU37240; -.
DR PaxDb; P45860; -.
DR PRIDE; P45860; -.
DR DNASU; 938453; -.
DR EnsemblBacteria; CAB15752; CAB15752; BSU_37240.
DR GeneID; 938453; -.
DR KEGG; bsu:BSU37240; -.
DR PATRIC; fig|224308.179.peg.4034; -.
DR eggNOG; COG1502; Bacteria.
DR InParanoid; P45860; -.
DR OMA; HMNINTK; -.
DR PhylomeDB; P45860; -.
DR BioCyc; BSUB:BSU37240-MON; -.
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; 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 2: Evidence at transcript 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..500
FT /note="Probable cardiolipin synthase YwiE"
FT /id="PRO_0000201247"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 31..51
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 237..264
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 413..440
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 242
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 418
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 420
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 425
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ SEQUENCE 500 AA; 58248 MW; 3BEF85FD4F0681B8 CRC64;
MLKRRLEFFF LYMMLIGAYV IWFFPVSRLE FYGGLLCYIS IILFSIYSLI LENRTSQHTL
LWIHILVFFP IVGYVFYLFS GQLYVKGKLF KTKRMYNREK LRKLFDKEET PEVTGLKDNQ
ERFFTYSIRA AHMNINTKSN IKVLKNGEET FPDIFKAMRK AESYIHIEYY MFKSDMLGRG
MMDIMMEKAR QGVEVRFLYD AAGSMKLARR DIMRMKQAGV DIVPFSPLKY GFFNQKLNFR
NHRKIVIIDG KTGFVGGLNV GKEYISRDPY IGFWRDTHLR LEGEIVQTLH AIFMLDWEYV
SNEVLIDQEE YNTPVPVEGG GIYQIVATGP DMKESMSDLY YEMISSAQKS IWIATPYFVP
NESIRTALKA AATKGVEVRV MVPEKNDSFL TQYASRSYFP ELLLEGIEVY SYQKGFMHQK
VMIIDGDLAS VGTANMDMRS FQLNFEVNVF FTDAEAIRTL EAHFEEDMQE SEKLSPVGFY
KRGVADRTKE SFARLFSGVL
