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CLP_XANOP
ID   CLP_XANOP               Reviewed;         230 AA.
AC   B2SL05;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=CRP-like protein Clp;
DE   AltName: Full=Catabolite activation-like protein;
DE            Short=CAP-like;
GN   Name=clp; OrderedLocusNames=PXO_04006;
OS   Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=360094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PXO99A;
RX   PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA   Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA   Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA   Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA   Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA   Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA   Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA   White F.F., Bogdanove A.J.;
RT   "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT   oryzae pv. oryzae PXO99A.";
RL   BMC Genomics 9:204-204(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACD57282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000967; ACD57282.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011260495.1; NC_010717.2.
DR   AlphaFoldDB; B2SL05; -.
DR   SMR; B2SL05; -.
DR   STRING; 360094.PXO_04006; -.
DR   EnsemblBacteria; ACD57282; ACD57282; PXO_04006.
DR   KEGG; xop:PXO_04006; -.
DR   eggNOG; COG0664; Bacteria.
DR   HOGENOM; CLU_075053_3_5_6; -.
DR   OrthoDB; 1596937at2; -.
DR   Proteomes; UP000001740; 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_0000405707"
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
 
 
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