ID   CLPX_METNO              Reviewed;         423 AA.
AC   B8IN27;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=Mnod_7406;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001349; ACL62143.1; -; Genomic_DNA.
DR   RefSeq; WP_015933701.1; NC_011894.1.
DR   AlphaFoldDB; B8IN27; -.
DR   SMR; B8IN27; -.
DR   STRING; 460265.Mnod_7406; -.
DR   EnsemblBacteria; ACL62143; ACL62143; Mnod_7406.
DR   KEGG; mno:Mnod_7406; -.
DR   eggNOG; COG1219; Bacteria.
DR   HOGENOM; CLU_014218_8_2_5; -.
DR   OMA; HYKRVQA; -.
DR   OrthoDB; 718259at2; -.
DR   Proteomes; UP000008207; 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..423
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_1000123841"
FT   DOMAIN          3..56
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         40
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   423 AA;  46397 MW;  58AF863A63ED0735 CRC64;
     MSKAGGNDSK STLYCSFCGK SQHEVRKLIA GPTVFICDEC VELCMDIIRE ESKSSLVKSR
     DGVPTPKEIR RVLDDYVIGQ DFAKKVLSVA VHNHYKRLAH AAKHNDVELA KSNILLIGPT
     GSGKTLLAQT LARILDVPFT MADATTLTEA GYVGEDVENI ILKLLQASDY NVERAQRGIV
     YIDEIDKISR KSDNPSITRD VSGEGVQQAL LKIMEGTVAS VPPQGGRKHP QQEFLQVDTT
     NILFICGGAF AGLERIISAR GKGTSIGFGA TVQAPDDRRT GEIFRNVEPE DLLKFGLIPE
     FVGRLPVLAT LEDLDEIALK RILQEPKNAL VKQYQRLFEM ENVDLTFQEE ALTLVARKAI
     ERKTGARGLR SILESILLET MYDLPGLDSV EQVVIGPEVV DGKARPLYIH GDRSKDAPAS
     VSA