位置:首页 > 蛋白库 > CLS1_BACSU
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024