CLP_XANC8
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 03-AUG-2022, entry version 105.
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; Proteobacteria; 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}.
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DR EMBL; CP000050; AAY47567.1; -; Genomic_DNA.
DR RefSeq; WP_011035725.1; NC_007086.1.
DR AlphaFoldDB; Q4UZF6; -.
DR SMR; Q4UZF6; -.
DR EnsemblBacteria; AAY47567; AAY47567; XC_0486.
DR GeneID; 58011784; -.
DR KEGG; xcb:XC_0486; -.
DR HOGENOM; CLU_075053_3_5_6; -.
DR OMA; FLEYCHI; -.
DR OrthoDB; 1596937at2; -.
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 transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP: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 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 c-
FT 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
