ID   CLP_XANCB               Reviewed;         230 AA.
AC   B0RN01;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=CRP-like protein Clp;
DE   AltName: Full=Catabolite activation-like protein;
DE            Short=CAP-like;
GN   Name=clp; OrderedLocusNames=xcc-b100_0502;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP49836.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RN01; -.
DR   SMR; B0RN01; -.
DR   KEGG; xca:xcc-b100_0502; -.
DR   HOGENOM; CLU_075053_3_5_6; -.
DR   OMA; FLEYCHI; -.
DR   Proteomes; UP000001188; 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; Repressor;
KW   Transcription; Transcription regulation; Virulence.
FT   CHAIN           1..230
FT                   /note="CRP-like protein Clp"
FT                   /id="PRO_0000405703"
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;  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