ID A0A543IV50_9ACTN Unreviewed; 427 AA.
AC A0A543IV50;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 18.
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 ORFNames=FHX40_1127 {ECO:0000313|EMBL:TQM74454.1};
OS Thermopolyspora flexuosa.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Thermopolyspora.
OX NCBI_TaxID=103836 {ECO:0000313|EMBL:TQM74454.1, ECO:0000313|Proteomes:UP000319213};
RN [1] {ECO:0000313|EMBL:TQM74454.1, ECO:0000313|Proteomes:UP000319213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43186 {ECO:0000313|EMBL:TQM74454.1,
RC ECO:0000313|Proteomes:UP000319213};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TQM74454.1}.
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; VFPQ01000001; TQM74454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A543IV50; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000319213; 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:TQM74454.1};
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:TQM74454.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000319213};
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 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 427 AA; 46966 MW; 9CEA5960B2C9933E CRC64;
MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL SESSELKWDN
LPKPREIYEF LDSYVIGQEK AKKALSVAVY NHYKRVQSGD RARDDGVELA KSNILLLGPT
GSGKTLLAQT LAKMLNVPFA IADATALTEA GYVGEDVENI LLKLIQAADY DVKKAETGII
YIDEVDKIAR KSENPSITRD VSGEGVQQAL LKILEGTTAS VPPQGGRKHP HQEFIQIDTT
NVLFICGGAF AGLEKIIEAR IGKKGIGFNA VIPSKKELDS SDIFAEVMPE DLLKYGMIPE
FIGRLPVITS VHNLDRDALI AILTEPKNAL VKQYRRLFEL DNVELEFTPD ALEAIADQAI
LRGTGARGLR AIMEEVLLSV MYEVPSRDDV ARVVITREAV LEHVNPTLVP RDQINVKQPR
TPREKSA
//