ID   CLP_XANOR               Reviewed;         230 AA.
AC   Q5GV61;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=CRP-like protein Clp;
DE   AltName: Full=Catabolite activation-like protein;
DE            Short=CAP-like;
GN   Name=clp; OrderedLocusNames=XOO4158;
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85;
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA   Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA   Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA   Go S.-J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
CC   -!- FUNCTION: Global transcriptional regulator that regulates virulence
CC       factors production by activating or repressing the expression of a
CC       large set of genes in diffusible signal factor (DSF) pathway.
CC       {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Allosterically inhibited by cyclic di-GMP (c-di-
CC       GMP), which binds to Clp and abolishes its ability to bind its target
CC       gene promoter. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: Binding of c-di-GMP appears to trigger the active Clp
CC       conformation into an open form or inactive state, hence abolishing its
CC       DNA-binding ability. {ECO:0000250}.
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DR   EMBL; AE013598; AAW77412.1; -; Genomic_DNA.
DR   RefSeq; WP_011260495.1; NC_006834.1.
DR   AlphaFoldDB; Q5GV61; -.
DR   SMR; Q5GV61; -.
DR   STRING; 291331.XOO4158; -.
DR   EnsemblBacteria; AAW77412; AAW77412; XOO4158.
DR   KEGG; xoo:XOO4158; -.
DR   HOGENOM; CLU_075053_3_5_6; -.
DR   OMA; FLEYCHI; -.
DR   Proteomes; UP000006735; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProtKB-KW.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS: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; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00325; Crp; 1.
DR   PRINTS; PR00034; HTHCRP.
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; PS00042; HTH_CRP_1; 1.
DR   PROSITE; PS51063; HTH_CRP_2; 1.
PE   3: Inferred from homology;
KW   Activator; Allosteric enzyme; c-di-GMP; Cytoplasm; DNA-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Virulence.
FT   CHAIN           1..230
FT                   /note="CRP-like protein Clp"
FT                   /id="PRO_0000405705"
FT   DOMAIN          158..230
FT                   /note="HTH crp-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   DNA_BIND        190..209
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   BINDING         18..139
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   230 AA;  25641 MW;  37AED762A9E640AA CRC64;
     MSSANTTVVT TTVRNATPSL ALDAGTIERF LAHSHRRRYP TRTDVFRPGD PAGTLYYVIS
     GSVSIIAEED DDRELVLGYF GSGEFVGEMG LFIESDTREV ILRTRTQCEL AEISYERLQQ
     LFQTSLSPDA PKILYAIGVQ LSKRLLDTTR KASRLAFLDV TDRIVRTLHD LSKEPEAMSH
     PQGTQLRVSR QELARLVGCS REMAGRVLKK LQADGLLHAR GKTVVLYGTR