GenomeNet

Database: UniProt
Entry: A0A0N9XG82_MYCFO
LinkDB: A0A0N9XG82_MYCFO
Original site: A0A0N9XG82_MYCFO 
ID   A0A0N9XG82_MYCFO        Unreviewed;       426 AA.
AC   A0A0N9XG82;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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:ALI27833.1};
GN   ORFNames=HGK73_31380 {ECO:0000313|EMBL:NOQ62537.1}, NCTC1542_02650
GN   {ECO:0000313|EMBL:STZ87878.1}, XA26_40210
GN   {ECO:0000313|EMBL:ALI27833.1};
OS   Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1766 {ECO:0000313|EMBL:ALI27833.1, ECO:0000313|Proteomes:UP000057134};
RN   [1] {ECO:0000313|EMBL:ALI27833.1, ECO:0000313|Proteomes:UP000057134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:ALI27833.1,
RC   ECO:0000313|Proteomes:UP000057134};
RX   PubMed=26507234; DOI=10.1128/mBio.01520-15;
RA   Costa K.C., Bergkessel M., Saunders S., Korlach J., Newman D.K.;
RT   "Enzymatic Degradation of Phenazines Can Generate Energy and Protect
RT   Sensitive Organisms from Toxicity.";
RL   MBio 6:e01520-e01515(2015).
RN   [2] {ECO:0000313|EMBL:STZ87878.1, ECO:0000313|Proteomes:UP000255389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC1542 {ECO:0000313|EMBL:STZ87878.1,
RC   ECO:0000313|Proteomes:UP000255389};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:NOQ62537.1, ECO:0000313|Proteomes:UP000565634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate_2 {ECO:0000313|EMBL:NOQ62537.1,
RC   ECO:0000313|Proteomes:UP000565634};
RA   Lin D.;
RT   "Rapid and easy defining the species of Mycobacterium based on whole genome
RT   sequences.";
RL   Submitted (DEC-2019) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011269; ALI27833.1; -; Genomic_DNA.
DR   EMBL; JAAZWM010000022; NOQ62537.1; -; Genomic_DNA.
DR   EMBL; UGQY01000003; STZ87878.1; -; Genomic_DNA.
DR   RefSeq; WP_003879920.1; NZ_VHPZ01000014.1.
DR   AlphaFoldDB; A0A0N9XG82; -.
DR   STRING; 1766.XA26_40210; -.
DR   KEGG; mft:XA26_40210; -.
DR   PATRIC; fig|1766.6.peg.3998; -.
DR   Proteomes; UP000057134; Chromosome.
DR   Proteomes; UP000255389; Unassembled WGS sequence.
DR   Proteomes; UP000565634; Unassembled WGS sequence.
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:NOQ62537.1};
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:NOQ62537.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057134};
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         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   426 AA;  46720 MW;  D77AEAE6DD5D0DB7 CRC64;
     MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL ADADDVKLDE
     LPKPAEIRDF LEGYVIGQDT AKRTLAVAVY NHYKRIQAGE KSRDSRSEPV ELTKSNILML
     GPTGCGKTYL AQTLAKMLNV PFAIADATAL TEAGYVGEDV ENILLKLIQA ADYDVKRAET
     GIIYIDEVDK IARKSENPSI TRDVSGEGVQ QALLKILEGT QASVPPQGGR KHPHQEFIQI
     DTTNVLFIVA GAFAGLEKIV SDRVGKRGLG FGAEVRSKAE IDTQDHFAEV MPEDLIKFGL
     IPEFIGRLPV VASVTNLDKD SLVKILSEPK NALVKQYVRL FEMDGVELEF TDEALEAIAD
     QAIHRGTGAR GLRAIMEEVL LPVMYDIPSR DDVAKVVVTK ETVQDNVLPT IVPRKPSRSE
     RRDKTA
//
DBGET integrated database retrieval system