ID A0A1W1I8Y8_9BACT Unreviewed; 423 AA.
AC A0A1W1I8Y8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:SLM49466.1};
GN ORFNames=NSJP_3299 {ECO:0000313|EMBL:SLM49466.1};
OS Nitrospira japonica.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1325564 {ECO:0000313|EMBL:SLM49466.1, ECO:0000313|Proteomes:UP000192042};
RN [1] {ECO:0000313|EMBL:SLM49466.1, ECO:0000313|Proteomes:UP000192042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Genome sequencing of Nitrospira japonica strain NJ11
RC {ECO:0000313|EMBL:SLM49466.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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}.
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DR EMBL; LT828648; SLM49466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1I8Y8; -.
DR STRING; 1325564.NSJP_3299; -.
DR KEGG; nja:NSJP_3299; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000192042; Chromosome i.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein 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; 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 SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW Hydrolase {ECO:0000313|EMBL:SLM49466.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW Protease {ECO:0000313|EMBL:SLM49466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192042};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 123..276
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 327..421
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 423 AA; 46550 MW; 390FE692A2ED7814 CRC64;
MFWDRVHPSP EPRPVCWFCG RSETTVRNLV ASPVEHSCKS CGVISKVLIC EECLQRSLNR
DRIGQPSTSS SLPSVIPKPT DIKATLDEFV IGQERAKKVL AVAVHNHYKR IVNRDRLKHV
GLQKGNILMI GSTGTGKTLL SQTLARILHV PFAIADATTL TEAGYVGEDV ENVVLKLLQN
CDYDVPRAET GIIYIDEIDK ISRKSESPSL TRDVSGEGVQ QALLKLVEGT TCNVPQKGGR
KHPEQEFIRV DTTDILFIAG GAFVGLDHII AERTMPKRLG FDMHDPSVGI DGHTEILGRV
RSEDLLKFGL IPEFVGRFPV LTTLADLDVP ALIRVLTEPR NALVKQYQAL FEIEGVELTF
SDSAVRAVAR RAALMKTGAR ALRTILEEVM LDLMYEVPAM GSVKSVEITE DVIAGTAQPR
VLS
//