ID   CLPX_LEPIN              Reviewed;         420 AA.
AC   Q8F353;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=LA_2558;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(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; AE010300; AAN49757.1; -; Genomic_DNA.
DR   RefSeq; NP_712739.1; NC_004342.2.
DR   RefSeq; WP_001085747.1; NC_004342.2.
DR   AlphaFoldDB; Q8F353; -.
DR   SMR; Q8F353; -.
DR   STRING; 189518.LA_2558; -.
DR   EnsemblBacteria; AAN49757; AAN49757; LA_2558.
DR   GeneID; 61144721; -.
DR   KEGG; lil:LA_2558; -.
DR   PATRIC; fig|189518.3.peg.2543; -.
DR   HOGENOM; CLU_014218_8_2_12; -.
DR   InParanoid; Q8F353; -.
DR   OMA; HYKRVQA; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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   GO; GO:0051301; P:cell division; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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..420
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_0000160377"
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         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   420 AA;  46562 MW;  A2367EA0F5AEBDB6 CRC64;
     MAKKTPGNNG KQKLFCSFCG KEQDAVKRLV AGPGVYICDE CISLCNEIIA EDHEHSHEKS
     EVFSEVPSPA DIKSILDQYV IGQDHAKKAL SVAVYNHYKR VNLKEKKSDV EIEKSNILLI
     GPTGSGKTLL AQTLARIIKV PFAIVDATAL TEAGYVGEDV ENIILKLIQN ADNDIKKAEV
     GIIYIDEVDK IARKSDSASI TRDVSGEGVQ QALLKIIEGT VANVPPQGGR KHPHQEYLQV
     DTKNILFILG GAFVDLPNII KSRTGIKTIG FGSEEQRIQS ENKDVLMEQV IPEDLIKFGL
     IPEFIGRLPI VATLQELNVD MLRQIFREPK NSVLKQYTRL LELENVKLTF HDEAIDKIAE
     LAIKRESGAR GLRAIVENIM LDLMFDIPSR KDIEEVIITA EVIANRVAPT LILKKESKIA