CRA_ECOLI
ID CRA_ECOLI Reviewed; 334 AA.
AC P0ACP1; P21168;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Catabolite repressor/activator;
DE AltName: Full=Fructose repressor;
GN Name=cra; Synonyms=fruC, fruR, shl; OrderedLocusNames=b0080, JW0078;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2198273; DOI=10.1128/jb.172.8.4696-4700.1990;
RA Leclerc G., Noel G., Drapeau G.R.;
RT "Molecular cloning, nucleotide sequence, and expression of shl, a new gene
RT in the 2-minute region of the genetic map of Escherichia coli.";
RL J. Bacteriol. 172:4696-4700(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1851954; DOI=10.1007/bf00273623;
RA Jahreis K., Postma P.W., Lengeler J.W.;
RT "Nucleotide sequence of the ilvH-fruR gene region of Escherichia coli K12
RT and Salmonella typhimurium LT2.";
RL Mol. Gen. Genet. 226:332-336(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RX PubMed=8230205; DOI=10.1006/jmbi.1993.1561;
RA Ramseier T.M., Negre D., Cortay J.C., Scarabel M., Cozzone A.J.,
RA Saier M.H. Jr.;
RT "In vitro binding of the pleiotropic transcriptional regulatory protein,
RT FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and
RT Salmonella typhimurium.";
RL J. Mol. Biol. 234:28-44(1993).
RN [7]
RP FUNCTION IN GLYOXYLATE SHUNT REGULATION, DNA-BINDING, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=8195118; DOI=10.1016/s0021-9258(17)36548-1;
RA Cortay J.C., Negre D., Scarabel M., Ramseier T.M., Vartak N.B., Reizer J.,
RA Saier M.H. Jr., Cozzone A.J.;
RT "In vitro asymmetric binding of the pleiotropic regulatory protein, FruR,
RT to the ace operator controlling glyoxylate shunt enzyme synthesis.";
RL J. Biol. Chem. 269:14885-14891(1994).
RN [8]
RP FUNCTION IN REGULATION OF CARBON METABOLISM.
RX PubMed=8577250; DOI=10.1111/j.1365-2958.1995.tb02339.x;
RA Ramseier T.M., Bledig S., Michotey V., Feghali R., Saier M.H. Jr.;
RT "The global regulatory protein FruR modulates the direction of carbon flow
RT in Escherichia coli.";
RL Mol. Microbiol. 16:1157-1169(1995).
RN [9]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=8550429; DOI=10.1128/jb.178.1.280-283.1996;
RA Bledig S.A., Ramseier T.M., Saier M.H. Jr.;
RT "Frur mediates catabolite activation of pyruvate kinase (pykF) gene
RT expression in Escherichia coli.";
RL J. Bacteriol. 178:280-283(1996).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=8858581; DOI=10.1046/j.1365-2958.1996.6341350.x;
RA Negre D., Bonod-Bidaud C., Geourjon C., Deleage G., Cozzone A.J.,
RA Cortay J.C.;
RT "Definition of a consensus DNA-binding site for the Escherichia coli
RT pleiotropic regulatory protein, FruR.";
RL Mol. Microbiol. 21:257-266(1996).
RN [11]
RP FUNCTION, AND GENE NAME.
RX PubMed=9084760; DOI=10.1016/0923-2508(96)84003-4;
RA Ramseier T.M.;
RT "Cra and the control of carbon flux via metabolic pathways.";
RL Res. Microbiol. 147:489-493(1996).
RN [12]
RP REVIEW.
RX PubMed=8655535; DOI=10.1128/jb.178.12.3411-3417.1996;
RA Saier M.H. Jr., Ramseier T.M.;
RT "The catabolite repressor/activator (Cra) protein of enteric bacteria.";
RL J. Bacteriol. 178:3411-3417(1996).
RN [13]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9371462; DOI=10.1128/jb.179.22.7129-7134.1997;
RA Mikulskis A., Aristarkhov A., Lin E.C.;
RT "Regulation of expression of the ethanol dehydrogenase gene (adhE) in
RT Escherichia coli by catabolite repressor activator protein Cra.";
RL J. Bacteriol. 179:7129-7134(1997).
RN [14]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16115199; DOI=10.1111/j.1365-2443.2005.00888.x;
RA Shimada T., Fujita N., Maeda M., Ishihama A.;
RT "Systematic search for the Cra-binding promoters using genomic SELEX
RT system.";
RL Genes Cells 10:907-918(2005).
RN [15]
RP STRUCTURE BY NMR OF 1-57.
RX PubMed=9237914; DOI=10.1006/jmbi.1997.1123;
RA Penin F., Geourjon C., Montserret R., Boeckmann A., Lesage A., Yang Y.S.,
RA Bonod-Bidaud C., Cortay J.-C., Negre D., Cozzone A.J., Deleage G.;
RT "Three-dimensional structure of the DNA-binding domain of the fructose
RT repressor from Escherichia coli by 1H and 15N NMR.";
RL J. Mol. Biol. 270:496-510(1997).
CC -!- FUNCTION: Global transcriptional regulator, which plays an important
CC role in the regulation of carbon metabolism. Activates transcription of
CC genes encoding biosynthetic and oxidative enzymes (involved in Krebs
CC cycle, glyoxylate shunt and gluconeogenesis, such as ppsA and fbp).
CC Represses genes involved in sugar catabolism, such as fruB, pfkA, pykF
CC and adhE. Binds asymmetrically to the two half-sites of its operator.
CC {ECO:0000269|PubMed:16115199, ECO:0000269|PubMed:8195118,
CC ECO:0000269|PubMed:8230205, ECO:0000269|PubMed:8550429,
CC ECO:0000269|PubMed:8577250, ECO:0000269|PubMed:8858581,
CC ECO:0000269|PubMed:9084760, ECO:0000269|PubMed:9371462}.
CC -!- ACTIVITY REGULATION: Is displaced from DNA by low concentrations of
CC fructose-1-phosphate. {ECO:0000269|PubMed:8230205}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8195118}.
CC -!- MISCELLANEOUS: Activation of transcription is observed when the Cra
CC operator is upstream of the RNA polymerase binding site. Inhibition of
CC transcription is observed when the operator overlaps or is downstream
CC of the RNA polymerase binding site (PubMed:8655535).
CC {ECO:0000305|PubMed:8655535}.
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DR EMBL; M35034; AAA24629.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38857.1; -; Genomic_DNA.
DR EMBL; X55457; CAA39104.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73191.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96648.1; -; Genomic_DNA.
DR PIR; JU0298; JU0298.
DR RefSeq; NP_414622.1; NC_000913.3.
DR RefSeq; WP_000762401.1; NZ_STEB01000010.1.
DR PDB; 1UXC; NMR; -; A=1-57.
DR PDB; 1UXD; NMR; -; A=1-57.
DR PDB; 2IKS; X-ray; 1.85 A; A/B=44-334.
DR PDBsum; 1UXC; -.
DR PDBsum; 1UXD; -.
DR PDBsum; 2IKS; -.
DR AlphaFoldDB; P0ACP1; -.
DR SMR; P0ACP1; -.
DR BioGRID; 4259359; 9.
DR BioGRID; 849205; 2.
DR DIP; DIP-35838N; -.
DR IntAct; P0ACP1; 12.
DR STRING; 511145.b0080; -.
DR jPOST; P0ACP1; -.
DR PaxDb; P0ACP1; -.
DR PRIDE; P0ACP1; -.
DR EnsemblBacteria; AAC73191; AAC73191; b0080.
DR EnsemblBacteria; BAB96648; BAB96648; BAB96648.
DR GeneID; 67416153; -.
DR GeneID; 944804; -.
DR KEGG; ecj:JW0078; -.
DR KEGG; eco:b0080; -.
DR PATRIC; fig|1411691.4.peg.2201; -.
DR EchoBASE; EB0334; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_0_6; -.
DR InParanoid; P0ACP1; -.
DR OMA; NSRKAGY; -.
DR PhylomeDB; P0ACP1; -.
DR BioCyc; EcoCyc:PD00521; -.
DR EvolutionaryTrace; P0ACP1; -.
DR PRO; PR:P0ACP1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009750; P:response to fructose; IEA:InterPro.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR012781; Fruct_sucro_rep.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF00532; Peripla_BP_1; 1.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR TIGRFAMs; TIGR02417; fruct_sucro_rep; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..334
FT /note="Catabolite repressor/activator"
FT /id="PRO_0000107945"
FT DOMAIN 1..58
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 3..22
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:1UXC"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:1UXC"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:1UXC"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:1UXC"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2IKS"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2IKS"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:2IKS"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 247..261
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 293..309
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2IKS"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:2IKS"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:2IKS"
SQ SEQUENCE 334 AA; 37999 MW; 503AE935CC2EC0C8 CRC64;
MKLDEIARLA GVSRTTASYV INGKAKQYRV SDKTVEKVMA VVREHNYHPN AVAAGLRAGR
TRSIGLVIPD LENTSYTRIA NYLERQARQR GYQLLIACSE DQPDNEMRCI EHLLQRQVDA
IIVSTSLPPE HPFYQRWAND PFPIVALDRA LDREHFTSVV GADQDDAEML AEELRKFPAE
TVLYLGALPE LSVSFLREQG FRTAWKDDPR EVHFLYANSY EREAAAQLFE KWLETHPMPQ
ALFTTSFALL QGVMDVTLRR DGKLPSDLAI ATFGDNELLD FLQCPVLAVA QRHRDVAERV
LEIVLASLDE PRKPKPGLTR IKRNLYRRGV LSRS
