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Entry version 133 (11 Dec 2019)
Sequence version 2 (11 Jul 2002)
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Protein

CRP-like protein Clp

Gene

clp

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. 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.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically inhibited by cyclic di-GMP (c-di-GMP), which binds to Clp and abolishes its ability to bind its target gene promoter.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi18 – 139cNMPAdd BLAST122
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi190 – 209H-T-H motifPROSITE-ProRule annotationAdd BLAST20

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
XCAM190485:XCC0472-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CRP-like protein Clp
Alternative name(s):
Catabolite activation-like protein
Short name:
CAP-like
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:clp
Ordered Locus Names:XCC0472
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri190485 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001010 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant produces less EPS and shows decrease in cellulase and protease activities.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi70D → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi99E → A: Decrease in DNA-binding. 1 Publication1
Mutagenesisi150R → A: Decrease in DNA-binding. 1 Publication1
Mutagenesisi154R → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi162D → A: Decrease in DNA-binding. 1 Publication1
Mutagenesisi165V → A: Decrease in DNA-binding. 1 Publication1
Mutagenesisi166R → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi170D → A: Almost no change in DNA-binding, but decrease in c-di-GMP-binding. 1 Publication1
Mutagenesisi195R → A: Decrease in DNA-binding. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001001521 – 230CRP-like protein ClpAdd BLAST230

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is induced by DSF signal, via the RpfC/RpfG two-component system.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
340.xcc-b100_0502

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1230
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P22260

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P22260

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini158 – 230HTH crp-typePROSITE-ProRule annotationAdd BLAST73

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107RYR Bacteria
COG0664 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000250565

KEGG Orthology (KO)

More...
KOi
K10914

Identification of Orthologs from Complete Genome Data

More...
OMAi
AKTECEV

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00038 CAP_ED, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit
2.60.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00027 cNMP_binding, 1 hit
PF00325 Crp, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00034 HTHCRP

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00100 cNMP, 1 hit
SM00419 HTH_CRP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit
SSF51206 SSF51206, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50042 CNMP_BINDING_3, 1 hit
PS00042 HTH_CRP_1, 1 hit
PS51063 HTH_CRP_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P22260-1 [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 11, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF9252D2A1D2C1F0B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti98R → H in AAA27597 (PubMed:2170330).Curated1
Sequence conflicti98R → H in AAA27598 (PubMed:1322886).Curated1
Sequence conflicti139V → A in AAD20599 (PubMed:11361081).Curated1
Sequence conflicti200 – 202SRE → CAQ in AAA27597 (PubMed:2170330).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M58745 Genomic DNA Translation: AAA27597.1
M92289 Genomic DNA Translation: AAA27598.1
AF111840 Genomic DNA Translation: AAD20599.1
AE008922 Genomic DNA Translation: AAM39790.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A42949

NCBI Reference Sequences

More...
RefSeqi
NP_635866.1, NC_003902.1
WP_011035725.1, NC_003902.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAM39790; AAM39790; XCC0472

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1000958
35543787

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xcc:XCC0472

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|190485.4.peg.519

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58745 Genomic DNA Translation: AAA27597.1
M92289 Genomic DNA Translation: AAA27598.1
AF111840 Genomic DNA Translation: AAD20599.1
AE008922 Genomic DNA Translation: AAM39790.1
PIRiA42949
RefSeqiNP_635866.1, NC_003902.1
WP_011035725.1, NC_003902.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IWZX-ray2.30A/B/C/D1-230[»]
SMRiP22260
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi340.xcc-b100_0502

Genome annotation databases

EnsemblBacteriaiAAM39790; AAM39790; XCC0472
GeneIDi1000958
35543787
KEGGixcc:XCC0472
PATRICifig|190485.4.peg.519

Phylogenomic databases

eggNOGiENOG4107RYR Bacteria
COG0664 LUCA
HOGENOMiHOG000250565
KOiK10914
OMAiAKTECEV

Enzyme and pathway databases

BioCyciXCAM190485:XCC0472-MONOMER

Miscellaneous databases

EvolutionaryTraceiP22260

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
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
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCLP_XANCP
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22260
Secondary accession number(s): Q9S6B5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 11, 2002
Last modified: December 11, 2019
This is version 133 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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