ID   CLPX_STRT2              Reviewed;         408 AA.
AC   Q5M5B0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=stu0581;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(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; CP000023; AAV60287.1; -; Genomic_DNA.
DR   RefSeq; WP_002950151.1; NC_006448.1.
DR   AlphaFoldDB; Q5M5B0; -.
DR   SMR; Q5M5B0; -.
DR   STRING; 264199.stu0581; -.
DR   EnsemblBacteria; AAV60287; AAV60287; stu0581.
DR   GeneID; 66898485; -.
DR   KEGG; stl:stu0581; -.
DR   eggNOG; COG1219; Bacteria.
DR   HOGENOM; CLU_014218_8_2_9; -.
DR   OMA; HYKRVQA; -.
DR   Proteomes; UP000001170; 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..408
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_1000024686"
FT   DOMAIN          1..53
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
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         34
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         118..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   408 AA;  45063 MW;  8E524411889B9EAE CRC64;
     MAGNRNEEMV YCSFCGKNQE EVKKIIAGNG VFICNECVAL SQEIIREETA EEVLADLAET
     PKPKELLDIL NNYVVGQDRV KRALAVAVYN HYKRINFTES REDNDVDLQK SNILMIGPTG
     SGKTYLAQTL ARSLNVPFAI ADATSLTEAG YVGEDVENIL LKLIQAADFN IERAERGIIY
     VDEIDKIAKK GENVSITRDV SGEGVQQALL KIIEGTVASV PPQGGRKHPN QEMIQIDTKN
     ILFIVGGAFD GIEDIVKQRL GEKIIGFGQN NKAIDDESSY MKEIVAEDIQ KFGLIPEFIG
     RLPVLATLEQ LTVDDLVRIL TEPRNALVKQ YQTLLSYDGV ELEFDQDALE AIASKAIERK
     TGARGLRSII EEVMMDVMFE IPSLEDVTKV RITKEAVDGK AAPVLETA