ID CLP_XANC8 Reviewed; 230 AA. AC Q4UZF6; DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=CRP-like protein Clp; DE AltName: Full=Catabolite activation-like protein; DE Short=CAP-like; GN Name=clp; OrderedLocusNames=XC_0486; OS Xanthomonas campestris pv. campestris (strain 8004). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=314565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8004; RX PubMed=15899963; DOI=10.1101/gr.3378705; RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R., RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.; RT "Comparative and functional genomic analyses of the pathogenicity of RT phytopathogen Xanthomonas campestris pv. campestris."; RL Genome Res. 15:757-767(2005). RN [2] RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-99 AND RP THR-149. RC STRAIN=8004; RX PubMed=20008070; DOI=10.1128/jb.01253-09; RA Tao F., He Y.W., Wu D.H., Swarup S., Zhang L.H.; RT "The cyclic nucleotide monophosphate domain of Xanthomonas campestris RT global regulator Clp defines a new class of cyclic di-GMP effectors."; RL J. Bacteriol. 192:1020-1029(2010). 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:0000269|PubMed:20008070}. 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:0000269|PubMed:20008070}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000050; AAY47567.1; -; Genomic_DNA. DR RefSeq; WP_011035725.1; NC_007086.1. DR AlphaFoldDB; Q4UZF6; -. DR SMR; Q4UZF6; -. DR GeneID; 58011784; -. DR KEGG; xcb:XC_0486; -. DR HOGENOM; CLU_075053_3_5_6; -. DR Proteomes; UP000000420; Chromosome. DR CollecTF; EXPREG_00000e30; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF. DR GO; GO:0003824; F:catalytic activity; IEA:UniProtKB-KW. DR GO; GO:0035438; F:cyclic-di-GMP 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:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEP:CollecTF. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR CDD; cd00038; CAP_ED; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. 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 PANTHER; PTHR24567:SF79; CAMP-ACTIVATED GLOBAL TRANSCRIPTIONAL REGULATOR CRP; 1. DR PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1. 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; SSF51206; cAMP-binding domain-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR PROSITE; PS00042; HTH_CRP_1; 1. DR PROSITE; PS51063; HTH_CRP_2; 1. PE 1: Evidence at protein level; KW Activator; Allosteric enzyme; c-di-GMP; Cytoplasm; DNA-binding; Repressor; KW Transcription; Transcription regulation; Virulence. FT CHAIN 1..230 FT /note="CRP-like protein Clp" FT /id="PRO_0000405702" 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" FT MUTAGEN 99 FT /note="E->S: No change in DNA-binding, but decrease in FT response to c-di-GMP." FT /evidence="ECO:0000269|PubMed:20008070" FT MUTAGEN 149 FT /note="T->S: No change in DNA-binding and in response to FT c-di-GMP." FT /evidence="ECO:0000269|PubMed:20008070" SQ SEQUENCE 230 AA; 25711 MW; F9252D2A1D2C1F0B CRC64; MSLGNTTVVT TTVRNATPSL TLDAGTIERF LAHSHRRRYP TRTDVFRPGD PAGTLYYVIS GSVSIIAEED DDRELVLGYF GSGEFVGEMG LFIESDTREV ILRTRTQCEL AEISYERLQQ LFQTSLSPDA PRILYAIGVQ LSKRLLDTTR KASRLAFLDV TDRIVRTLHD LSKEPEAMSH PQGTQLRVSR QELARLVGCS REMAGRVLKK LQADGLLHAR GKTVVLYGTR //