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
//