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CSPA_ECOLI
ID   CSPA_ECOLI              Reviewed;          70 AA.
AC   P0A9X9; P15277; P37410; Q2M7L7; Q54170;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Cold shock protein CspA;
DE            Short=CSP-A;
DE   AltName: Full=7.4 kDa cold shock protein;
DE   AltName: Full=CS7.4 {ECO:0000303|PubMed:2404279};
GN   Name=cspA; Synonyms=cspS; OrderedLocusNames=b3556, JW3525;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-23, SUBCELLULAR
RP   LOCATION, AND INDUCTION BY COLD-SHOCK.
RC   STRAIN=K12 / SB221;
RX   PubMed=2404279; DOI=10.1073/pnas.87.1.283;
RA   Goldstein J., Pollitt N.S., Inouye M.;
RT   "Major cold shock protein of Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:283-287(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1597410; DOI=10.1128/jb.174.12.3867-3873.1992;
RA   Tanabe H., Goldstein J., Yang M., Inouye M.;
RT   "Identification of the promoter region of the Escherichia coli major cold
RT   shock gene, cspA.";
RL   J. Bacteriol. 174:3867-3873(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-60.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=9439003; DOI=10.1038/sj.jim.2900463;
RA   Francis K.P., Stewart G.S.A.B.;
RT   "Detection and speciation of bacteria through PCR using universal major
RT   cold-shock protein primer oligomers.";
RL   J. Ind. Microbiol. Biotechnol. 19:286-293(1997).
RN   [7]
RP   FUNCTION.
RX   PubMed=1961761; DOI=10.1073/pnas.88.23.10907;
RA   la Teana A., Brandi A., Falconi M., Spurio R., Pon C.L., Gualerzi C.O.;
RT   "Identification of a cold shock transcriptional enhancer of the Escherichia
RT   coli gene encoding nucleoid protein H-NS.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10907-10911(1991).
RN   [8]
RP   INDUCTION BY COLD-SHOCK.
RC   STRAIN=CSH142;
RX   PubMed=8898389; DOI=10.1111/j.1365-2958.1996.tb02582.x;
RA   Jones P.G., Inouye M.;
RT   "RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose
RT   absence triggers the cold-shock response.";
RL   Mol. Microbiol. 21:1207-1218(1996).
RN   [9]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [10]
RP   STRUCTURE BY NMR.
RX   PubMed=7515185; DOI=10.1073/pnas.91.11.5114;
RA   Newkirk K., Feng W., Jiang W., Tejero R., Emerson S.D., Inouye M.,
RA   Montelione G.T.;
RT   "Solution NMR structure of the major cold shock protein (CspA) from
RT   Escherichia coli: identification of a binding epitope for DNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5114-5118(1994).
RN   [11]
RP   STRUCTURE BY NMR.
RX   PubMed=9692981; DOI=10.1021/bi980269j;
RA   Feng W., Tejero R., Zimmerman D.E., Inouye M., Montelione G.T.;
RT   "Solution NMR structure and backbone dynamics of the major cold-shock
RT   protein (CspA) from Escherichia coli: evidence for conformational dynamics
RT   in the single-stranded RNA-binding site.";
RL   Biochemistry 37:10881-10896(1998).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8197194; DOI=10.1073/pnas.91.11.5119;
RA   Schindelin H., Jiang W., Inouye M., Heinemann U.;
RT   "Crystal structure of CspA, the major cold shock protein of Escherichia
RT   coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5119-5123(1994).
CC   -!- FUNCTION: Binds to and stimulates the transcription of the CCAAT-
CC       containing, cold-shock-inducible promoters of the H-NS and GyrA
CC       proteins. Binds also to the inverted repeat 5'-ATTGG-3'.
CC       {ECO:0000269|PubMed:1961761}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2404279}.
CC   -!- INDUCTION: In response to low temperature (at protein level)
CC       (PubMed:2404279, PubMed:8898389). {ECO:0000269|PubMed:2404279,
CC       ECO:0000269|PubMed:8898389}.
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DR   EMBL; M30139; AAA23617.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18533.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76580.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77739.1; -; Genomic_DNA.
DR   EMBL; U60035; AAC80239.1; -; Genomic_DNA.
DR   PIR; JH0201; OCECJ.
DR   RefSeq; NP_418012.1; NC_000913.3.
DR   RefSeq; WP_000014594.1; NZ_STEB01000018.1.
DR   PDB; 1MJC; X-ray; 2.00 A; A=2-70.
DR   PDB; 2BH8; X-ray; 1.90 A; A/B=2-36.
DR   PDB; 2L15; NMR; -; A=1-70.
DR   PDB; 3MEF; NMR; -; A=2-70.
DR   PDBsum; 1MJC; -.
DR   PDBsum; 2BH8; -.
DR   PDBsum; 2L15; -.
DR   PDBsum; 3MEF; -.
DR   AlphaFoldDB; P0A9X9; -.
DR   BMRB; P0A9X9; -.
DR   SMR; P0A9X9; -.
DR   BioGRID; 4262533; 15.
DR   BioGRID; 852378; 2.
DR   DIP; DIP-31862N; -.
DR   IntAct; P0A9X9; 42.
DR   STRING; 511145.b3556; -.
DR   jPOST; P0A9X9; -.
DR   PaxDb; P0A9X9; -.
DR   PRIDE; P0A9X9; -.
DR   EnsemblBacteria; AAC76580; AAC76580; b3556.
DR   EnsemblBacteria; BAE77739; BAE77739; BAE77739.
DR   GeneID; 64293021; -.
DR   GeneID; 67517040; -.
DR   GeneID; 948070; -.
DR   KEGG; ecj:JW3525; -.
DR   KEGG; eco:b3556; -.
DR   PATRIC; fig|1411691.4.peg.3158; -.
DR   EchoBASE; EB0164; -.
DR   eggNOG; COG1278; Bacteria.
DR   HOGENOM; CLU_117621_2_1_6; -.
DR   InParanoid; P0A9X9; -.
DR   OMA; GPCANKV; -.
DR   PhylomeDB; P0A9X9; -.
DR   BioCyc; EcoCyc:PD03695; -.
DR   EvolutionaryTrace; P0A9X9; -.
DR   PRO; PR:P0A9X9; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR   GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IDA:EcoliWiki.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoliWiki.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:EcoliWiki.
DR   GO; GO:0001072; F:transcription antitermination factor activity, RNA binding; IDA:EcoliWiki.
DR   GO; GO:0060567; P:negative regulation of DNA-templated transcription, termination; IDA:EcoliWiki.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0009409; P:response to cold; IEP:EcoliWiki.
DR   CDD; cd04458; CSP_CDS; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012156; Cold_shock_CspA.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR019844; CSD_1.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF00313; CSD; 1.
DR   PIRSF; PIRSF002599; Cold_shock_A; 1.
DR   PRINTS; PR00050; COLDSHOCK.
DR   SMART; SM00357; CSP; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS00352; CSD_1; 1.
DR   PROSITE; PS51857; CSD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Reference proteome; Stress response; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2404279"
FT   CHAIN           2..70
FT                   /note="Cold shock protein CspA"
FT                   /id="PRO_0000100233"
FT   DOMAIN          7..67
FT                   /note="CSD"
FT   STRAND          5..13
FT                   /evidence="ECO:0007829|PDB:2BH8"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:2BH8"
FT   STRAND          18..27
FT                   /evidence="ECO:0007829|PDB:2BH8"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:2BH8"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:1MJC"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1MJC"
FT   STRAND          50..56
FT                   /evidence="ECO:0007829|PDB:1MJC"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1MJC"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:1MJC"
SQ   SEQUENCE   70 AA;  7403 MW;  CED47F00BF18A49B CRC64;
     MSGKMTGIVK WFNADKGFGF ITPDDGSKDV FVHFSAIQND GYKSLDEGQK VSFTIESGAK
     GPAAGNVTSL
 
 
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