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CDSA_SHIFL
ID   CDSA_SHIFL              Reviewed;         285 AA.
AC   P0ABG3; P06466;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Phosphatidate cytidylyltransferase;
DE            EC=2.7.7.41;
DE   AltName: Full=CDP-DAG synthase;
DE   AltName: Full=CDP-DG synthase;
DE   AltName: Full=CDP-diacylglycerol synthase;
DE            Short=CDS;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase;
DE   AltName: Full=CDP-diglyceride synthase;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN   Name=cdsA; OrderedLocusNames=SF0165, S0168;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC         diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN41827.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP15708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN41827.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP15708.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_706120.4; NC_004337.2.
DR   RefSeq; WP_000922446.1; NZ_WPGW01000006.1.
DR   AlphaFoldDB; P0ABG3; -.
DR   SMR; P0ABG3; -.
DR   STRING; 198214.SF0165; -.
DR   EnsemblBacteria; AAN41827; AAN41827; SF0165.
DR   EnsemblBacteria; AAP15708; AAP15708; S0168.
DR   GeneID; 1024478; -.
DR   GeneID; 66671537; -.
DR   KEGG; sfl:SF0165; -.
DR   KEGG; sfx:S0168; -.
DR   PATRIC; fig|198214.7.peg.187; -.
DR   HOGENOM; CLU_037294_1_2_6; -.
DR   OrthoDB; 1533756at2; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR000374; PC_trans.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Nucleotidyltransferase; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..285
FT                   /note="Phosphatidate cytidylyltransferase"
FT                   /id="PRO_0000090746"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   285 AA;  31454 MW;  0D77DCD5EC5FBA9F CRC64;
     MLKYRLISAF VLIPVVIAAL FLLPPVGFAI VTLVVCMLAA WEWGQLSGFT TRSQRVWLAV
     LCGLLLALML FLLPEYHRNI HQPLVEISLW ASLGWWIVAL LLVLFYPGSA AIWRNSKTLR
     LIFGVLTIVP FFWGMLALRA WHYDENHYSG AIWLLYVMIL VWGADSGAYM FGKLFGKHKL
     APKVSPGKTW QGFIGGLATA AVISWGYGMW ANLDVAPVTL LICSIVAALA SVLGDLTESM
     FKREAGIKDS GHLIPGHGGI LDRIDSLTAA VPVFACLLLL VFRTL
 
 
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