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Q9L7X5 (CLPX_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. 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:
ATP-dependent Clp protease ATP-binding subunit ClpX
Gene names
Name:clpX
Ordered Locus Names:BruAb1_1114
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP By similarity. HAMAP-Rule MF_00175

Subunit structure

Heterodimer of ClpP and ClpX By similarity. HAMAP-Rule MF_00175

Sequence similarities

Belongs to the ClpX chaperone family.

Ontologies

Keywords
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChaperone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424ATP-dependent Clp protease ATP-binding subunit ClpX HAMAP-Rule MF_00175
PRO_0000160325

Regions

Zinc finger17 – 4226C4-type HAMAP-Rule MF_00175
Nucleotide binding120 – 1278ATP Potential

Experimental info

Sequence conflict68 – 703PQE → RRQ in AAF32319. Ref.1
Sequence conflict1781Missing Ref.1
Sequence conflict1801G → S Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9L7X5 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 6A68089A37209608

FASTA42446,656
        10         20         30         40         50         60 
MSKVSNGGGD SKNTLYCSFC GKSQHEVRKL IAGPTVFICD ECVELCMDII REENKSSMVK 

        70         80         90        100        110        120 
SREGVPTPQE IMAVLDDYVI GQKDAKRVLS VAVHNHYKRL AHQSKNSDIE LAKSNILLVG 

       130        140        150        160        170        180 
PTGCGKTYLA QTLARIIDVP FIMADATTLT EAGYVGEDVE NIILKLLQAA DYNVERAQRG 

       190        200        210        220        230        240 
IVYIDEVDKI SRKSDNPSIT RDVSGEGVQQ ALLKIMEGTV ASVPPQGGRK HPQQEFLQVD 

       250        260        270        280        290        300 
TTNILFICGG AFAGLDRIIS ARGEKTSIGF GATVKSVDER RIGEVFKELE PEDLLKFGLI 

       310        320        330        340        350        360 
PEFVGRLPVI ATLEDLDVDA LVQILTEPKN ALVKQYQRLF DMENVELVFH DDALRAIANK 

       370        380        390        400        410        420 
AVERKTGARG LRSIMEKILL DTMFELPTLE GVREVVISGD VVDGSARPLY IYAERQDEKG 


NVSA 

« Hide

References

« Hide 'large scale' references
[1]"The Brucella abortus clpP and clpX are not subject to classical heat shock regulation and are critical for cell viability."
Robertson G.T., Roop R.M. II
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF218420 Genomic DNA. Translation: AAF32319.1.
AE017223 Genomic DNA. Translation: AAX74455.1.
RefSeqYP_221816.1. NC_006932.1.

3D structure databases

ProteinModelPortalQ9L7X5.
SMRQ9L7X5. Positions 11-53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb1_1114.

Proteomic databases

PRIDEQ9L7X5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX74455; AAX74455; BruAb1_1114.
GeneID3340036.
KEGGbmb:BruAb1_1114.
PATRIC17823917. VBIBruAbo15061_1181.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1219.
HOGENOMHOG000010093.
KOK03544.
OMALDTMFDL.
OrthoDBEOG625JZK.
ProtClustDBPRK05342.

Enzyme and pathway databases

BioCycBABO262698:GJC2-1136-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_00175. ClpX.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR019489. Clp_ATPase_C.
IPR004487. Clp_protease_ATP-bd_su_ClpX.
IPR027417. P-loop_NTPase.
IPR010603. Znf_CppX_C4.
[Graphical view]
PfamPF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
PF06689. zf-C4_ClpX. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
SM00994. zf-C4_ClpX. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00382. clpX. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCLPX_BRUAB
AccessionPrimary (citable) accession number: Q9L7X5
Secondary accession number(s): Q57D29
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 81 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

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names