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Protein

CRP-like protein Clp

Gene

clp

Organism
Xanthomonas campestris pv. campestris (strain 8004)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

Allosterically inhibited by cyclic di-GMP (c-di-GMP), which binds to Clp and abolishes its ability to bind its target gene promoter.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 139cNMPAdd BLAST122
DNA bindingi190 – 209H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

  • catalytic activity Source: UniProtKB-KW
  • cyclic-di-GMP binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • pathogenesis Source: UniProtKB-KW
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation, Virulence
Ligandc-di-GMP

Names & Taxonomyi

Protein namesi
Recommended name:
CRP-like protein Clp
Alternative name(s):
Catabolite activation-like protein
Short name:
CAP-like
Gene namesi
Name:clp
Ordered Locus Names:XC_0486
OrganismiXanthomonas campestris pv. campestris (strain 8004)
Taxonomic identifieri314565 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
Proteomesi
  • UP000000420 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi99E → S: No change in DNA-binding, but decrease in response to c-di-GMP. 1 Publication1
Mutagenesisi149T → S: No change in DNA-binding and in response to c-di-GMP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004057021 – 230CRP-like protein ClpAdd BLAST230

Expressioni

Gene expression databases

CollecTFiEXPREG_00000e30.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi314565.XC_0486.

Structurei

3D structure databases

ProteinModelPortaliQ4UZF6.
SMRiQ4UZF6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini158 – 230HTH crp-typePROSITE-ProRule annotationAdd BLAST73

Domaini

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.By similarity

Phylogenomic databases

eggNOGiCOG0664. LUCA.
HOGENOMiHOG000250565.
KOiK10914.
OMAiCAHEICR.
OrthoDBiPOG091H00WB.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProiView protein in InterPro
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR012318. HTH_CRP.
IPR014710. RmlC-like_jellyroll.
IPR018335. Tscrpt_reg_HTH_Crp-type_CS.
IPR011991. WHTH_DNA-bd_dom.
PfamiView protein in Pfam
PF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
PRINTSiPR00034. HTHCRP.
SMARTiView protein in SMART
SM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51206. SSF51206. 1 hit.
PROSITEiView protein in PROSITE
PS50042. CNMP_BINDING_3. 1 hit.
PS00042. HTH_CRP_1. 1 hit.
PS51063. HTH_CRP_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q4UZF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLGNTTVVT TTVRNATPSL TLDAGTIERF LAHSHRRRYP TRTDVFRPGD
60 70 80 90 100
PAGTLYYVIS GSVSIIAEED DDRELVLGYF GSGEFVGEMG LFIESDTREV
110 120 130 140 150
ILRTRTQCEL AEISYERLQQ LFQTSLSPDA PRILYAIGVQ LSKRLLDTTR
160 170 180 190 200
KASRLAFLDV TDRIVRTLHD LSKEPEAMSH PQGTQLRVSR QELARLVGCS
210 220 230
REMAGRVLKK LQADGLLHAR GKTVVLYGTR
Length:230
Mass (Da):25,711
Last modified:July 5, 2005 - v1
Checksum:iF9252D2A1D2C1F0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000050 Genomic DNA. Translation: AAY47567.1.
RefSeqiWP_011035725.1. NC_007086.1.

Genome annotation databases

EnsemblBacteriaiAAY47567; AAY47567; XC_0486.
KEGGixcb:XC_0486.
PATRICi24062214. VBIXanCam24967_0519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000050 Genomic DNA. Translation: AAY47567.1.
RefSeqiWP_011035725.1. NC_007086.1.

3D structure databases

ProteinModelPortaliQ4UZF6.
SMRiQ4UZF6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi314565.XC_0486.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAY47567; AAY47567; XC_0486.
KEGGixcb:XC_0486.
PATRICi24062214. VBIXanCam24967_0519.

Phylogenomic databases

eggNOGiCOG0664. LUCA.
HOGENOMiHOG000250565.
KOiK10914.
OMAiCAHEICR.
OrthoDBiPOG091H00WB.

Gene expression databases

CollecTFiEXPREG_00000e30.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProiView protein in InterPro
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR012318. HTH_CRP.
IPR014710. RmlC-like_jellyroll.
IPR018335. Tscrpt_reg_HTH_Crp-type_CS.
IPR011991. WHTH_DNA-bd_dom.
PfamiView protein in Pfam
PF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
PRINTSiPR00034. HTHCRP.
SMARTiView protein in SMART
SM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51206. SSF51206. 1 hit.
PROSITEiView protein in PROSITE
PS50042. CNMP_BINDING_3. 1 hit.
PS00042. HTH_CRP_1. 1 hit.
PS51063. HTH_CRP_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCLP_XANC8
AccessioniPrimary (citable) accession number: Q4UZF6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: July 5, 2005
Last modified: March 15, 2017
This is version 80 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.