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Database: UniProt
Entry: A0A1W1I8Y8_9BACT
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Original site: A0A1W1I8Y8_9BACT 
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
//
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