CRPL_CORGL
ID CRPL_CORGL Reviewed; 227 AA.
AC Q79VI7; Q93PX6;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=CRP-like cAMP-activated global transcriptional regulator {ECO:0000250|UniProtKB:P9WMH3};
DE AltName: Full=cAMP receptor protein {ECO:0000250|UniProtKB:P9WMH3};
DE Short=CRP {ECO:0000250|UniProtKB:P9WMH3};
DE AltName: Full=cAMP regulatory protein {ECO:0000250|UniProtKB:P9WMH3};
GN Name=glxR {ECO:0000303|PubMed:15150232}; OrderedLocusNames=cg0350, Cgl0291;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nakagawa S.;
RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15150232; DOI=10.1128/jb.186.11.3453-3460.2004;
RA Kim H.J., Kim T.H., Kim Y., Lee H.S.;
RT "Identification and characterization of glxR, a gene involved in regulation
RT of glyoxylate bypass in Corynebacterium glutamicum.";
RL J. Bacteriol. 186:3453-3460(2004).
RN [5]
RP FUNCTION.
RX PubMed=16385030; DOI=10.1128/jb.188.2.409-423.2006;
RA Letek M., Valbuena N., Ramos A., Ordonez E., Gil J.A., Mateos L.M.;
RT "Characterization and use of catabolite-repressed promoters from gluconate
RT genes in Corynebacterium glutamicum.";
RL J. Bacteriol. 188:409-423(2006).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=18355281; DOI=10.1111/j.1574-6968.2008.01098.x;
RA Jungwirth B., Emer D., Brune I., Hansmeier N., Puehler A., Eikmanns B.J.,
RA Tauch A.;
RT "Triple transcriptional control of the resuscitation promoting factor 2
RT (rpf2) gene of Corynebacterium glutamicum by the regulators of acetate
RT metabolism RamA and RamB and the cAMP-dependent regulator GlxR.";
RL FEMS Microbiol. Lett. 281:190-197(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH CAMP, AND SUBUNIT.
RA Jungwirth B., Pojer F.;
RT "Crystal structure of GlxR transcription factor from Corynebacterium
RT glutamicum with cAMP.";
RL Submitted (MAR-2011) to the PDB data bank.
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS), DNA-BINDING, AND SUBUNIT.
RX PubMed=25469635; DOI=10.1371/journal.pone.0113265;
RA Townsend P.D., Jungwirth B., Pojer F., Bussmann M., Money V.A., Cole S.T.,
RA Puhler A., Tauch A., Bott M., Cann M.J., Pohl E.;
RT "The crystal structures of apo and cAMP-bound GlxR from Corynebacterium
RT glutamicum reveal structural and dynamic changes upon cAMP binding in
RT CRP/FNR family transcription factors.";
RL PLoS ONE 9:E113265-E113265(2014).
CC -!- FUNCTION: Global transcriptional regulator that complexes with cAMP and
CC binds to specific DNA promoter sites, causing DNA-bending, to regulate
CC transcription. cAMP improves binding to specific DNA sequences,
CC probably by altering protein conformation. Involved in the regulation
CC of gntP and gntK genes, which are involved in gluconate metabolism
CC (PubMed:16385030). May form dimers which bind to the aceB promoter
CC region in the presence of cAMP and repress the glyoxylate bypass genes
CC (PubMed:15150232). It could be a positive regulator of rpf2 gene
CC expression during growth on acetate as the sole carbon source, however
CC because the cytosolic cAMP level is elevated in the presence of glucose
CC and low upon growth on acetate, it is conceivable that it is unable to
CC function as an activator under acetate conditions (PubMed:18355281).
CC {ECO:0000269|PubMed:15150232, ECO:0000269|PubMed:16385030,
CC ECO:0000269|PubMed:18355281}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15150232,
CC ECO:0000269|PubMed:25469635, ECO:0000269|Ref.7}.
CC -!- INDUCTION: Seems to repress its own expression.
CC {ECO:0000269|PubMed:18355281}.
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DR EMBL; BA000036; BAB97684.1; -; Genomic_DNA.
DR EMBL; BX927148; CAF18861.1; -; Genomic_DNA.
DR RefSeq; NP_599543.1; NC_003450.3.
DR RefSeq; WP_003855810.1; NC_006958.1.
DR PDB; 3R6S; X-ray; 2.38 A; A/B/C/D/E/F=1-227.
DR PDB; 4BYY; X-ray; 2.48 A; A/B=1-227.
DR PDBsum; 3R6S; -.
DR PDBsum; 4BYY; -.
DR AlphaFoldDB; Q79VI7; -.
DR SMR; Q79VI7; -.
DR STRING; 196627.cg0350; -.
DR PRIDE; Q79VI7; -.
DR GeneID; 58310258; -.
DR KEGG; cgb:cg0350; -.
DR KEGG; cgl:Cgl0291; -.
DR PATRIC; fig|196627.13.peg.295; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_3_4_11; -.
DR OMA; VLCRDFG; -.
DR Proteomes; UP000000582; Chromosome.
DR CollecTF; EXPREG_00000f90; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000874; P:regulation of glyoxylate cycle; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13545; HTH_Crp_2; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; cAMP; cAMP-binding; DNA-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..227
FT /note="CRP-like cAMP-activated global transcriptional
FT regulator"
FT /id="PRO_0000433043"
FT DOMAIN 147..220
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 180..199
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT BINDING 67..73
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0ACJ8"
FT BINDING 82..85
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 92..93
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 137..138
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 145..146
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0ACJ8"
FT BINDING 181..191
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0ACJ8"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4BYY"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 120..146
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3R6S"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3R6S"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:3R6S"
SQ 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
