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CRP-like cAMP-activated global transcriptional regulator (cAMP receptor protein) (CRP) (cAMP regulatory protein)

 CRPL_CORGL              Reviewed;         227 AA.
Q79VI7; Q93PX6;
27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 114.
RecName: Full=CRP-like cAMP-activated global transcriptional regulator {ECO:0000250|UniProtKB:P9WMH3};
AltName: Full=cAMP receptor protein {ECO:0000250|UniProtKB:P9WMH3};
Short=CRP {ECO:0000250|UniProtKB:P9WMH3};
AltName: Full=cAMP regulatory protein {ECO:0000250|UniProtKB:P9WMH3};
Name=glxR {ECO:0000303|PubMed:15150232};
OrderedLocusNames=cg0350, Cgl0291;
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
LMG 3730 / NCIMB 10025).
Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
Corynebacterium.
NCBI_TaxID=196627;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Nakagawa S.;
"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
Ikeda M., Nakagawa S.;
"The Corynebacterium glutamicum genome: features and impacts on
biotechnological processes.";
Appl. Microbiol. Biotechnol. 62:99-109(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence
and its impact on the production of L-aspartate-derived amino acids
and vitamins.";
J. Biotechnol. 104:5-25(2003).
[4]
FUNCTION, AND SUBUNIT.
PubMed=15150232; DOI=10.1128/JB.186.11.3453-3460.2004;
Kim H.J., Kim T.H., Kim Y., Lee H.S.;
"Identification and characterization of glxR, a gene involved in
regulation of glyoxylate bypass in Corynebacterium glutamicum.";
J. Bacteriol. 186:3453-3460(2004).
[5]
FUNCTION.
PubMed=16385030; DOI=10.1128/JB.188.2.409-423.2006;
Letek M., Valbuena N., Ramos A., Ordonez E., Gil J.A., Mateos L.M.;
"Characterization and use of catabolite-repressed promoters from
gluconate genes in Corynebacterium glutamicum.";
J. Bacteriol. 188:409-423(2006).
[6]
FUNCTION, AND INDUCTION.
PubMed=18355281; DOI=10.1111/j.1574-6968.2008.01098.x;
Jungwirth B., Emer D., Brune I., Hansmeier N., Puehler A.,
Eikmanns B.J., Tauch A.;
"Triple transcriptional control of the resuscitation promoting factor
2 (rpf2) gene of Corynebacterium glutamicum by the regulators of
acetate metabolism RamA and RamB and the cAMP-dependent regulator
GlxR.";
FEMS Microbiol. Lett. 281:190-197(2008).
[7]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH CAMP, AND
SUBUNIT.
Jungwirth B., Pojer F.;
"Crystal structure of GlxR transcription factor from Corynebacterium
glutamicum with cAMP.";
Submitted (MAR-2011) to the PDB data bank.
[8]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS), DNA-BINDING, AND SUBUNIT.
PubMed=25469635; DOI=10.1371/journal.pone.0113265;
Townsend P.D., Jungwirth B., Pojer F., Bussmann M., Money V.A.,
Cole S.T., Puhler A., Tauch A., Bott M., Cann M.J., Pohl E.;
"The crystal structures of apo and cAMP-bound GlxR from
Corynebacterium glutamicum reveal structural and dynamic changes upon
cAMP binding in CRP/FNR family transcription factors.";
PLoS ONE 9:E113265-E113265(2014).
-!- FUNCTION: Global transcriptional regulator that complexes with
cAMP and binds to specific DNA promoter sites, causing DNA-
bending, to regulate transcription. cAMP improves binding to
specific DNA sequences, probably by altering protein conformation.
Involved in the regulation of gntP and gntK genes, which are
involved in gluconate metabolism (PubMed:16385030). May form
dimers which bind to the aceB promoter region in the presence of
cAMP and repress the glyoxylate bypass genes (PubMed:15150232). It
could be a positive regulator of rpf2 gene expression during
growth on acetate as the sole carbon source, however because the
cytosolic cAMP level is elevated in the presence of glucose and
low upon growth on acetate, it is conceivable that it is unable to
function as an activator under acetate conditions
(PubMed:18355281). {ECO:0000269|PubMed:15150232,
ECO:0000269|PubMed:16385030, ECO:0000269|PubMed:18355281}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15150232,
ECO:0000269|PubMed:25469635, ECO:0000269|Ref.7}.
-!- INDUCTION: Seems to repress its own expression.
{ECO:0000269|PubMed:18355281}.
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EMBL; BA000036; BAB97684.1; -; Genomic_DNA.
EMBL; BX927148; CAF18861.1; -; Genomic_DNA.
RefSeq; NP_599543.1; NC_003450.3.
RefSeq; WP_003855810.1; NC_006958.1.
PDB; 3R6S; X-ray; 2.38 A; A/B/C/D/E/F=1-227.
PDB; 4BYY; X-ray; 2.48 A; A/B=1-227.
PDBsum; 3R6S; -.
PDBsum; 4BYY; -.
ProteinModelPortal; Q79VI7; -.
SMR; Q79VI7; -.
STRING; 196627.cg0350; -.
EnsemblBacteria; BAB97684; BAB97684; BAB97684.
EnsemblBacteria; CAF18861; CAF18861; cg0350.
GeneID; 1021325; -.
KEGG; cgb:cg0350; -.
KEGG; cgl:NCgl0286; -.
PATRIC; fig|196627.13.peg.295; -.
eggNOG; ENOG4105IJJ; Bacteria.
eggNOG; COG0664; LUCA.
HOGENOM; HOG000250566; -.
KO; K10914; -.
OMA; TECEVAE; -.
BioCyc; CORYNE:G18NG-9847-MONOMER; -.
Proteomes; UP000000582; Chromosome.
CollecTF; EXPREG_00000f90; -.
GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
GO; GO:0001216; F:bacterial-type RNA polymerase transcriptional activator activity, sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0001217; F:bacterial-type RNA polymerase transcriptional repressor activity, sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:CollecTF.
GO; GO:2000874; P:regulation of glyoxylate cycle; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00038; CAP_ED; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR012318; HTH_CRP.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF13545; HTH_Crp_2; 1.
SMART; SM00100; cNMP; 1.
SMART; SM00419; HTH_CRP; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS51063; HTH_CRP_2; 1.
1: Evidence at protein level;
3D-structure; Activator; cAMP; cAMP-binding; Complete proteome;
DNA-binding; Kinase; Nucleotide-binding; Reference proteome;
Repressor; Transcription; Transcription regulation; Transferase.
CHAIN 1 227 CRP-like cAMP-activated global
transcriptional regulator.
/FTId=PRO_0000433043.
DOMAIN 147 220 HTH crp-type. {ECO:0000255|PROSITE-
ProRule:PRU00387}.
NP_BIND 67 73 cAMP 1. {ECO:0000250|UniProtKB:P0ACJ8}.
NP_BIND 82 85 cAMP 1. {ECO:0000269|Ref.7}.
NP_BIND 92 93 cAMP 1. {ECO:0000269|Ref.7}.
NP_BIND 137 138 cAMP 1. {ECO:0000269|Ref.7}.
NP_BIND 145 146 cAMP 2. {ECO:0000250|UniProtKB:P0ACJ8}.
DNA_BIND 180 199 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00387}.
NP_BIND 181 191 cAMP 2. {ECO:0000250|UniProtKB:P0ACJ8}.
HELIX 4 9 {ECO:0000244|PDB:3R6S}.
HELIX 12 14 {ECO:0000244|PDB:3R6S}.
HELIX 19 27 {ECO:0000244|PDB:3R6S}.
STRAND 29 34 {ECO:0000244|PDB:3R6S}.
STRAND 39 41 {ECO:0000244|PDB:3R6S}.
STRAND 50 56 {ECO:0000244|PDB:3R6S}.
STRAND 58 63 {ECO:0000244|PDB:3R6S}.
STRAND 65 67 {ECO:0000244|PDB:4BYY}.
STRAND 69 75 {ECO:0000244|PDB:3R6S}.
STRAND 80 82 {ECO:0000244|PDB:3R6S}.
HELIX 84 87 {ECO:0000244|PDB:3R6S}.
STRAND 93 100 {ECO:0000244|PDB:3R6S}.
STRAND 102 107 {ECO:0000244|PDB:3R6S}.
HELIX 109 118 {ECO:0000244|PDB:3R6S}.
HELIX 120 146 {ECO:0000244|PDB:3R6S}.
HELIX 149 164 {ECO:0000244|PDB:3R6S}.
STRAND 166 168 {ECO:0000244|PDB:3R6S}.
STRAND 171 174 {ECO:0000244|PDB:3R6S}.
HELIX 180 187 {ECO:0000244|PDB:3R6S}.
HELIX 191 203 {ECO:0000244|PDB:3R6S}.
STRAND 206 209 {ECO:0000244|PDB:3R6S}.
STRAND 214 216 {ECO:0000244|PDB:3R6S}.
HELIX 219 225 {ECO:0000244|PDB:3R6S}.
SEQUENCE 227 AA; 24988 MW; 80D89C13246FD71D CRC64;
MEGVQEILSR AGIFQGVDPT AVNNLIQDME TVRFPRGATI FDEGEPGDRL YIITSGKVKL
ARHAPDGREN LLTIMGPSDM FGELSIFDPG PRTSSAVCVT EVHAATMNSD MLRNWVADHP
AIAEQLLRVL ARRLRRTNAS LADLIFTDVP GRVAKTLLQL ANRFGTQEAG ALRVNHDLTQ
EEIAQLVGAS RETVNKALAT FAHRGWIRLE GKSVLIVDTE HLARRAR


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