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Database: UniProt
Entry: A0A1E7MZF7_KITAU
LinkDB: A0A1E7MZF7_KITAU
Original site: A0A1E7MZF7_KITAU 
ID   A0A1E7MZF7_KITAU        Unreviewed;       429 AA.
AC   A0A1E7MZF7; A0A8H9HWV7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, 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:GGU96417.1};
GN   ORFNames=GCM10010502_58120 {ECO:0000313|EMBL:GGU96417.1}, HS99_0037740
GN   {ECO:0000313|EMBL:OEV33818.1}, K8W00_26090
GN   {ECO:0000313|EMBL:HJD84874.1};
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1894 {ECO:0000313|EMBL:OEV33818.1, ECO:0000313|Proteomes:UP000037395};
RN   [1] {ECO:0000313|EMBL:OEV33818.1, ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV33818.1}, and ATCC 10762 / DSM
RC   40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843 / NCIMB 8234 /
RC   A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC   12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, assembly and comparative genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OEV33818.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV33818.1};
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, Assembly and Comparative Genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:GGU96417.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU96417.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [5] {ECO:0000313|EMBL:GGU96417.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU96417.1};
RA   Sun Q., Ohkuma M.;
RL   Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:HJD84874.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ChiBjej1-411 {ECO:0000313|EMBL:HJD84874.1};
RX   PubMed=33868800;
RA   Gilroy R., Ravi A., Getino M., Pursley I., Horton D.L., Alikhan N.F.,
RA   Baker D., Gharbi K., Hall N., Watson M., Adriaenssens E.M.,
RA   Foster-Nyarko E., Jarju S., Secka A., Antonio M., Oren A., Chaudhuri R.R.,
RA   La Ragione R., Hildebrand F., Pallen M.J.;
RT   "Extensive microbial diversity within the chicken gut microbiome revealed
RT   by metagenomics and culture.";
RL   PeerJ 9:0-0(2021).
RN   [7] {ECO:0000313|EMBL:HJD84874.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ChiBjej1-411 {ECO:0000313|EMBL:HJD84874.1};
RA   Gilroy R.;
RL   Submitted (SEP-2021) 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:OEV33818.1}.
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DR   EMBL; BMUB01000018; GGU96417.1; -; Genomic_DNA.
DR   EMBL; DYYO01000126; HJD84874.1; -; Genomic_DNA.
DR   EMBL; JPRF03000057; OEV33818.1; -; Genomic_DNA.
DR   RefSeq; WP_030283761.1; NZ_LBHA01000513.1.
DR   AlphaFoldDB; A0A1E7MZF7; -.
DR   STRING; 1894.ADK78_22785; -.
DR   GeneID; 33986501; -.
DR   OMA; HYKRVQA; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000037395; Unassembled WGS sequence.
DR   Proteomes; UP000610124; Unassembled WGS sequence.
DR   Proteomes; UP000707501; 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:OEV33818.1};
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:OEV33818.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037395};
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         125..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   429 AA;  47000 MW;  16DA8C7FCA59D47E CRC64;
     MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL AETSEVRFEE
     LPKPREIYEF LDQYVVGQDL AKKALSVAVY NHYKRVQAGE AGRSGGNGRE DAIELAKSNI
     LLLGPTGSGK TLLAQTLARM LNVPFAIADA TALTEAGYVG EDVENILLKL IQAADYDVKK
     AETGIIYIDE IDKVARKSEN PSITRDVSGE GVQQALLKIL EGTTASVPPQ GGRKHPHQEF
     IQIDTTNVLF IVGGAFAGLE RIIEGRAGAK GIGFGANIRS KRESDASDHF RQVMPEDLVK
     FGMIPEFIGR LPVITSVHNL DREALLQILT EPKNALVKQY RKLFELDGVE LEFSRDALEA
     IADQAILRGT GARGLRAIME EVLMSVMYEV PSRQDVARVV VTGDVVSKHA IPTLVPRDMI
     KRERRDKSA
//
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