ID   CLPX_CLOTE              Reviewed;         431 AA.
AC   Q891J8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=CTC_02374;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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; AE015927; AAO36847.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q891J8; -.
DR   SMR; Q891J8; -.
DR   STRING; 212717.CTC_02374; -.
DR   PRIDE; Q891J8; -.
DR   EnsemblBacteria; AAO36847; AAO36847; CTC_02374.
DR   KEGG; ctc:CTC_02374; -.
DR   HOGENOM; CLU_014218_8_2_9; -.
DR   OMA; HYKRVQA; -.
DR   Proteomes; UP000001412; 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..431
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_0000160344"
FT   DOMAIN          2..55
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   REGION          405..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         118..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   431 AA;  47961 MW;  9F23C854587DDEC2 CRC64;
     MDMAKNDDKK QLKCSFCGKK QDQVKRLVAG PGVYICDECI ELCSEIITDE LEEDINTDMS
     SLPKPSEIKS YLDDYVIGQD DAKKALSVAV YNHYKRINLN NVNDDVELQK SNILLLGPTG
     SGKTLLAQTM AKFLNVPFAI ADATTLTEAG YVGEDVENIL LKLIQNADYD IEKAERGIIY
     IDEIDKIARK SENPSITRDV SGEGVQQSLL KILEGTIASV PPQGGRKHPH QEFIQLNTTN
     ILFICGGAFD GVDKLIERRT RNSSLGFGAD IKSKRDENVG ELLKKIMPED LLKFGLIPEF
     IGRLPITVTL SALDRDALVE ILTEPKNALV KQYKKLFEMD NVHLEFKEEA LKAIAEEAIR
     RSTGARGLRS IIEEIMKDIM FEIPSDESIS KVIINEETVS NKNPELIEAE GGKRPPIKIK
     KPRAKKGNET A