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Q9L7X5

- CLPX_BRUAB

UniProt

Q9L7X5 - CLPX_BRUAB

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Protein

ATP-dependent Clp protease ATP-binding subunit ClpX

Gene

clpX

Organism
Brucella abortus biovar 1 (strain 9-941)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri17 – 4226C4-typeUniRule annotationAdd
BLAST
Nucleotide bindingi121 – 1288ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein folding Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBABO262698:GJC2-1136-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent Clp protease ATP-binding subunit ClpXUniRule annotation
Gene namesi
Name:clpXUniRule annotation
Ordered Locus Names:BruAb1_1114
OrganismiBrucella abortus biovar 1 (strain 9-941)
Taxonomic identifieri262698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000540: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424ATP-dependent Clp protease ATP-binding subunit ClpXPRO_0000160325Add
BLAST

Proteomic databases

PRIDEiQ9L7X5.

Interactioni

Subunit structurei

Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.UniRule annotation

Protein-protein interaction databases

STRINGi262698.BruAb1_1114.

Structurei

3D structure databases

ProteinModelPortaliQ9L7X5.
SMRiQ9L7X5. Positions 11-53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ClpX chaperone family.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri17 – 4226C4-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1219.
HOGENOMiHOG000010093.
KOiK03544.
OMAiKLFSMEG.
OrthoDBiEOG625JZK.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00175. ClpX.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004487. Clp_protease_ATP-bd_su_ClpX.
IPR027417. P-loop_NTPase.
IPR010603. Znf_CppX_C4.
[Graphical view]
PfamiPF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
PF06689. zf-C4_ClpX. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
SM00994. zf-C4_ClpX. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00382. clpX. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9L7X5 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKVSNGGGD SKNTLYCSFC GKSQHEVRKL IAGPTVFICD ECVELCMDII
60 70 80 90 100
REENKSSMVK SREGVPTPQE IMAVLDDYVI GQKDAKRVLS VAVHNHYKRL
110 120 130 140 150
AHQSKNSDIE LAKSNILLVG PTGCGKTYLA QTLARIIDVP FIMADATTLT
160 170 180 190 200
EAGYVGEDVE NIILKLLQAA DYNVERAQRG IVYIDEVDKI SRKSDNPSIT
210 220 230 240 250
RDVSGEGVQQ ALLKIMEGTV ASVPPQGGRK HPQQEFLQVD TTNILFICGG
260 270 280 290 300
AFAGLDRIIS ARGEKTSIGF GATVKSVDER RIGEVFKELE PEDLLKFGLI
310 320 330 340 350
PEFVGRLPVI ATLEDLDVDA LVQILTEPKN ALVKQYQRLF DMENVELVFH
360 370 380 390 400
DDALRAIANK AVERKTGARG LRSIMEKILL DTMFELPTLE GVREVVISGD
410 420
VVDGSARPLY IYAERQDEKG NVSA
Length:424
Mass (Da):46,656
Last modified:June 21, 2005 - v2
Checksum:i6A68089A37209608
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 703PQE → RRQ in AAF32319. 1 PublicationCurated
Sequence conflicti178 – 1781Missing1 PublicationCurated
Sequence conflicti180 – 1801G → S1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF218420 Genomic DNA. Translation: AAF32319.1.
AE017223 Genomic DNA. Translation: AAX74455.1.
RefSeqiYP_221816.1. NC_006932.1.

Genome annotation databases

EnsemblBacteriaiAAX74455; AAX74455; BruAb1_1114.
GeneIDi3340036.
KEGGibmb:BruAb1_1114.
PATRICi17823917. VBIBruAbo15061_1181.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF218420 Genomic DNA. Translation: AAF32319.1 .
AE017223 Genomic DNA. Translation: AAX74455.1 .
RefSeqi YP_221816.1. NC_006932.1.

3D structure databases

ProteinModelPortali Q9L7X5.
SMRi Q9L7X5. Positions 11-53.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262698.BruAb1_1114.

Proteomic databases

PRIDEi Q9L7X5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAX74455 ; AAX74455 ; BruAb1_1114 .
GeneIDi 3340036.
KEGGi bmb:BruAb1_1114.
PATRICi 17823917. VBIBruAbo15061_1181.

Phylogenomic databases

eggNOGi COG1219.
HOGENOMi HOG000010093.
KOi K03544.
OMAi KLFSMEG.
OrthoDBi EOG625JZK.

Enzyme and pathway databases

BioCyci BABO262698:GJC2-1136-MONOMER.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
HAMAPi MF_00175. ClpX.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004487. Clp_protease_ATP-bd_su_ClpX.
IPR027417. P-loop_NTPase.
IPR010603. Znf_CppX_C4.
[Graphical view ]
Pfami PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
PF06689. zf-C4_ClpX. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
SM00994. zf-C4_ClpX. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00382. clpX. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCLPX_BRUAB
AccessioniPrimary (citable) accession number: Q9L7X5
Secondary accession number(s): Q57D29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 21, 2005
Last modified: October 29, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella abortus strain 9-941
    Brucella abortus (strain 9-941): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3