ID   CLPX1_METCA             Reviewed;         422 AA.
AC   Q60C67;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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}; Synonyms=clpX-1;
GN   OrderedLocusNames=MCA0243;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU90604.1; -; Genomic_DNA.
DR   RefSeq; WP_010959608.1; NC_002977.6.
DR   AlphaFoldDB; Q60C67; -.
DR   SMR; Q60C67; -.
DR   STRING; 243233.MCA0243; -.
DR   PRIDE; Q60C67; -.
DR   EnsemblBacteria; AAU90604; AAU90604; MCA0243.
DR   KEGG; mca:MCA0243; -.
DR   eggNOG; COG1219; Bacteria.
DR   HOGENOM; CLU_014218_8_2_6; -.
DR   OMA; KKVECNE; -.
DR   OrthoDB; 718259at2; -.
DR   Proteomes; UP000006821; 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..422
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX
FT                   1"
FT                   /id="PRO_0000160382"
FT   DOMAIN          4..57
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         120..127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   422 AA;  46437 MW;  B9F82F260D12D428 CRC64;
     MNEDRKNRES GKLLYCSFCG KSQHEVRKLI AGPAVFVCDE CVELCNDIIR EDLQGSEAGG
     VEGLPKPKEM KAILDQYVIG QDKAKRILSV AVYNHYKRLK ARTFRNDVEL AKSNVLLIGP
     TGSGKTLLAE TLARVLDVPF TIADATTLTE AGYVGEDVEN IIQKLLLACD YDVEKAEQGI
     VYIDEIDKIS RKADSPSITR DVSGEGVQQA LLKLMEGTVA SVPPQGGRKH PQQEFLQVNT
     ANILFICGGA FAGLDKTIRS RSERSGIGFS AEVKSKEENT NVGEILAGVE AEDLIRYGLI
     PEFIGRLPVV ATLEELDEAA LVRILIEPKN ALVKQYARLF EMEGCELEIL PEALGAIARR
     AMERKTGARG LRTIIEHALL DTMYELPSAE DVGKVVVDAK VIRGETEPHR VYRSVERQRV
     SA