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Database: UniProt
Entry: A0A1X0DQ92_9MYCO
LinkDB: A0A1X0DQ92_9MYCO
Original site: A0A1X0DQ92_9MYCO 
ID   A0A1X0DQ92_9MYCO        Unreviewed;       424 AA.
AC   A0A1X0DQ92;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175,
GN   ECO:0000313|EMBL:BBZ67950.1};
GN   ORFNames=BST26_00105 {ECO:0000313|EMBL:ORA74030.1}, MINS_33790
GN   {ECO:0000313|EMBL:BBZ67950.1};
OS   Mycolicibacterium insubricum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=444597 {ECO:0000313|EMBL:ORA74030.1, ECO:0000313|Proteomes:UP000192801};
RN   [1] {ECO:0000313|EMBL:ORA74030.1, ECO:0000313|Proteomes:UP000192801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45130 {ECO:0000313|EMBL:ORA74030.1,
RC   ECO:0000313|Proteomes:UP000192801};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BBZ67950.1, ECO:0000313|Proteomes:UP000466223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16366 {ECO:0000313|EMBL:BBZ67950.1,
RC   ECO:0000313|Proteomes:UP000466223};
RA   Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA   Iida T., Fujita J., Nakamura S.;
RT   "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT   species based on 7547 genomic profiles.";
RL   Emerg. Microbes Infect. 8:1043-1053(2019).
RN   [3] {ECO:0000313|EMBL:BBZ67950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 16366 {ECO:0000313|EMBL:BBZ67950.1};
RA   Matsumoto Y., Motooka D., Nakamura S.;
RL   Submitted (FEB-2020) 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:0000256|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:0000256|HAMAP-Rule:MF_00175}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC       Rule:MF_00175, ECO:0000256|PROSITE-ProRule:PRU01250}.
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DR   EMBL; AP022618; BBZ67950.1; -; Genomic_DNA.
DR   EMBL; MVHS01000001; ORA74030.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0DQ92; -.
DR   STRING; 444597.BST26_00105; -.
DR   KEGG; mij:MINS_33790; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000192801; Unassembled WGS sequence.
DR   Proteomes; UP000466223; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW   Hydrolase {ECO:0000313|EMBL:ORA74030.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00175}; Protease {ECO:0000313|EMBL:ORA74030.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192801};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          1..54
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         120..127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   424 AA;  46257 MW;  B843C5967D7DA300 CRC64;
     MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL ADADDVKLDE
     LPKPAEIREF LESYVIGQDA AKRTLAVAVY NHYKRIQAGE KSRGGEAVEL AKSNILMLGP
     TGCGKTYLAQ TLAKMLNVPF AIADATALTE AGYVGEDVEN ILLKLIQAAD YDVKRAETGI
     IYIDEVDKIA RKSENPSITR DVSGEGVQQA LLKILEGTQA SVPPQGGRKH PHQEFIQIDT
     TNVLFIVAGA FAGLEKIVSD RVGKRGLGFG AEVHSKADID TADHFAEVMP EDLIKFGLIP
     EFIGRLPVVA SVTNLDKESL VKILSEPKNA LVKQYVRLFE MDGVELEFTD EALEAVADQA
     IHRGTGARGL RAIMEEVLLP VMYDIPSRDD VAKVVVTQET VEDNVLPTIV PRKPSRSERR
     DKTA
//
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