CLPX1_WOLSU
ID CLPX1_WOLSU Reviewed; 417 AA.
AC Q7MAS4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX 1 {ECO:0000255|HAMAP-Rule:MF_00175};
GN Name=clpX1 {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=WS0058;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
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DR EMBL; BX571657; CAE09227.1; -; Genomic_DNA.
DR RefSeq; WP_011138027.1; NC_005090.1.
DR AlphaFoldDB; Q7MAS4; -.
DR SMR; Q7MAS4; -.
DR STRING; 273121.WS0058; -.
DR PRIDE; Q7MAS4; -.
DR EnsemblBacteria; CAE09227; CAE09227; WS0058.
DR KEGG; wsu:WS0058; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_7; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 718259at2; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 1.
DR HAMAP; MF_00175; ClpX; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR046425; ClpX_bact.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF06689; zf-C4_ClpX; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SMART; SM00994; zf-C4_ClpX; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..417
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX
FT 1"
FT /id="PRO_0000160457"
FT DOMAIN 1..47
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 417 AA; 46491 MW; 15EA11DF9F479E16 CRC64;
MNSRQCSFCR AKETKTNPLI AGNSVYICKN CVISAYKILF GEMERESDPL PEEEEGIDYI
PTPKELKSAL DEYVIGQERA KKVFSVAVYN HYKRIFKKEL LEEEDETEIS KSNILLIGPT
GSGKTLMAQT LARFLNVPIA ICDATSLTEA GYVGEDVENI LTRLLQAAEG DVKKAERGIV
FIDEIDKISR LSENRSITRD VSGEGVQQAL LKIIEGSVVN VPPKGGRKHP NQDFVQIDTS
QILFICGGAF DGMIELIKRR MGGNSLGFHG DKKGKSEESA LLHLVEPDDL VSYGLIPELI
GRLHVITTLD EITKEAMLEI LTKPKNALVK QYQKLFTMDE AELSFEPEAL EAIAELAIKR
KTGARGLRAI IEEVTLDLMY DLPELKEYEV IITKECVENR DAKPLLIKKK KNGKKSA