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P22260 (CLP_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CRP-like protein Clp
Alternative name(s):
Catabolite activation-like protein
Short name=CAP-like
Gene names
Name:clp
Ordered Locus Names:XCC0472
OrganismXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]
Taxonomic identifier190485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Global transcriptional regulator that regulates virulence factors production by activating or repressing the expression of a large set of genes in diffusible signal factor (DSF) pathway. It includes, among others, genes involved in extracellular polysaccharide (EPS) synthesis, flagellum synthesis, protein and fatty acid metabolism, multidrug resistance, iron uptake or genes encoding extracellular enzymes, membrane components and a few transcription factors. Regulation can be direct or indirect, via regulation of other transcriptional regulators. Not involved in DSF-mediated biofilm dispersal. Ref.5

Enzyme regulation

Allosterically inhibited by cyclic di-GMP (c-di-GMP), which binds to Clp and abolishes its ability to bind its target gene promoter. Ref.6 Ref.7

Subunit structure

Homodimer. Ref.7

Subcellular location

Cytoplasm Potential.

Induction

Expression is induced by DSF signal, via the RpfC/RpfG two-component system. Ref.5 Ref.6 Ref.7

Domain

Binding of c-di-GMP appears to trigger the active Clp conformation into an open form or inactive state, hence abolishing its DNA-binding ability. Ref.7

Disruption phenotype

Mutant produces less EPS and shows decrease in cellulase and protease activities. Ref.5

Sequence similarities

Contains 1 cyclic nucleotide-binding domain.

Contains 1 HTH crp-type DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230CRP-like protein Clp
PRO_0000100152

Regions

Domain158 – 23073HTH crp-type
Nucleotide binding18 – 139122cNMP
DNA binding190 – 20920H-T-H motif By similarity

Experimental info

Mutagenesis701D → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. Ref.7
Mutagenesis991E → A: Decrease in DNA-binding. Ref.7
Mutagenesis1501R → A: Decrease in DNA-binding. Ref.7
Mutagenesis1541R → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. Ref.7
Mutagenesis1621D → A: Decrease in DNA-binding. Ref.7
Mutagenesis1651V → A: Decrease in DNA-binding. Ref.7
Mutagenesis1661R → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. Ref.7
Mutagenesis1701D → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. Ref.7
Mutagenesis1951R → A: Decrease in DNA-binding. Ref.7
Sequence conflict981R → H in AAA27597. Ref.1
Sequence conflict981R → H in AAA27598. Ref.2
Sequence conflict1391V → A in AAD20599. Ref.3
Sequence conflict200 – 2023SRE → CAQ in AAA27597. Ref.1

Secondary structure

....................................... 230
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22260 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: F9252D2A1D2C1F0B

FASTA23025,711
        10         20         30         40         50         60 
MSLGNTTVVT TTVRNATPSL TLDAGTIERF LAHSHRRRYP TRTDVFRPGD PAGTLYYVIS 

        70         80         90        100        110        120 
GSVSIIAEED DDRELVLGYF GSGEFVGEMG LFIESDTREV ILRTRTQCEL AEISYERLQQ 

       130        140        150        160        170        180 
LFQTSLSPDA PRILYAIGVQ LSKRLLDTTR KASRLAFLDV TDRIVRTLHD LSKEPEAMSH 

       190        200        210        220        230 
PQGTQLRVSR QELARLVGCS REMAGRVLKK LQADGLLHAR GKTVVLYGTR 

« Hide

References

« Hide 'large scale' references
[1]"A Xanthomonas campestris pv. campestris protein similar to catabolite activation factor is involved in regulation of phytopathogenicity."
de Crecy-Lagard V., Glaser P., Lejeune P., Sismeiro O., Barber C.E., Daniels M.J., Danchin A.
J. Bacteriol. 172:5877-5883(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13951 / NCIB 11803 / NRRL B-1459.
[2]"DNA binding specificity and sequence of Xanthomonas campestris catabolite gene activator protein-like protein."
Dong Q., Ebright R.H.
J. Bacteriol. 174:5457-5461(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The early stages of filamentous phage phiLf infection require the host transcription factor, Clp."
Lee T.C., Chen S.T., Lee M.C., Chang C.M., Chen C.H., Weng S.F., Tseng Y.H.
J. Mol. Microbiol. Biotechnol. 3:471-481(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Xc17.
[4]"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. expand/collapse author list , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33913 / NCPPB 528 / LMG 568.
[5]"Xanthomonas campestris cell-cell communication involves a putative nucleotide receptor protein Clp and a hierarchical signalling network."
He Y.W., Ng A.Y., Xu M., Lin K., Wang L.H., Dong Y.H., Zhang L.H.
Mol. Microbiol. 64:281-292(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
Strain: Xc1.
[6]"The cyclic nucleotide monophosphate domain of Xanthomonas campestris global regulator Clp defines a new class of cyclic di-GMP effectors."
Tao F., He Y.W., Wu D.H., Swarup S., Zhang L.H.
J. Bacteriol. 192:1020-1029(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, ENZYME REGULATION.
Strain: 8004.
[7]"The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris."
Chin K.H., Lee Y.C., Tu Z.L., Chen C.H., Tseng Y.H., Yang J.M., Ryan R.P., McCarthy Y., Dow J.M., Wang A.H., Chou S.H.
J. Mol. Biol. 396:646-662(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), DNA-BINDING, ENZYME REGULATION, SUBUNIT, DOMAIN, MUTAGENESIS OF ASP-70; GLU-99; ARG-150; ARG-154; ASP-162; VAL-165; ARG-166; ASP-170 AND ARG-195.
Strain: Xc17.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58745 Genomic DNA. Translation: AAA27597.1.
M92289 Genomic DNA. Translation: AAA27598.1.
AF111840 Genomic DNA. Translation: AAD20599.1.
AE008922 Genomic DNA. Translation: AAM39790.1.
PIRA42949.
RefSeqNP_635866.1. NC_003902.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IWZX-ray2.30A/B/C/D1-230[»]
ProteinModelPortalP22260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190485.XCC0472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM39790; AAM39790; XCC0472.
GeneID1000958.
KEGGxcc:XCC0472.
PATRIC24071563. VBIXanCam115730_0519.

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000250565.
KOK10914.
OMAIMAEEDD.
OrthoDBEOG69GZGV.

Enzyme and pathway databases

BioCycXCAM190485:GIXZ-472-MONOMER.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR012318. HTH_CRP_2.
IPR014710. RmlC-like_jellyroll.
IPR001808. Tscrpt_reg_HTH_Crp.
IPR018335. Tscrpt_reg_HTH_Crp-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view]
PRINTSPR00034. HTHCRP.
SMARTSM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 1 hit.
PROSITEPS50042. CNMP_BINDING_3. 1 hit.
PS00042. HTH_CRP_1. 1 hit.
PS51063. HTH_CRP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22260.

Entry information

Entry nameCLP_XANCP
AccessionPrimary (citable) accession number: P22260
Secondary accession number(s): Q9S6B5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 11, 2002
Last modified: May 14, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references