ID A0A0K9EVY7_9ACTO Unreviewed; 422 AA.
AC A0A0K9EVY7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:VDG76863.1};
GN ORFNames=ACU19_00815 {ECO:0000313|EMBL:KMY24072.1}, ACU21_00510
GN {ECO:0000313|EMBL:OCA95885.1}, NCTC10327_01496
GN {ECO:0000313|EMBL:VDG76863.1}, SAMN05421878_101169
GN {ECO:0000313|EMBL:SDE03472.1};
OS Actinobaculum suis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=1657 {ECO:0000313|EMBL:KMY24072.1, ECO:0000313|Proteomes:UP000037036};
RN [1] {ECO:0000313|EMBL:KMY24072.1, ECO:0000313|Proteomes:UP000037036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U311 {ECO:0000313|EMBL:KMY24072.1,
RC ECO:0000313|Proteomes:UP000037036};
RA Moreno L.Z., Amigo C.R., Gobbi D.S., Ferreira T.S., Santos A.P.,
RA Moreno A.M.;
RT "Draft genome sequences of Brazilian Actinobaculum suis isolated from urine
RT and preputial swab.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OCA95885.1, ECO:0000313|Proteomes:UP000093494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1-9-1 {ECO:0000313|EMBL:OCA95885.1,
RC ECO:0000313|Proteomes:UP000093494};
RA Moreno L.Z., Amigo C.R., Moreno A.M.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SDE03472.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 20639 {ECO:0000313|EMBL:SDE03472.1};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000182744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20639 {ECO:0000313|Proteomes:UP000182744};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:VDG76863.1, ECO:0000313|Proteomes:UP000269974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10327 {ECO:0000313|EMBL:VDG76863.1,
RC ECO:0000313|Proteomes:UP000269974};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 ---------------------------------------------------------------------------
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; LFUS01000002; KMY24072.1; -; Genomic_DNA.
DR EMBL; MASY01000012; OCA95885.1; -; Genomic_DNA.
DR EMBL; FNAU01000001; SDE03472.1; -; Genomic_DNA.
DR EMBL; UYIO01000001; VDG76863.1; -; Genomic_DNA.
DR RefSeq; WP_049618789.1; NZ_UYIO01000001.1.
DR AlphaFoldDB; A0A0K9EVY7; -.
DR STRING; 1657.ACU20_00515; -.
DR PATRIC; fig|1657.3.peg.827; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000037036; Unassembled WGS sequence.
DR Proteomes; UP000093494; Unassembled WGS sequence.
DR Proteomes; UP000182744; Unassembled WGS sequence.
DR Proteomes; UP000269974; 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:KMY24072.1};
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:KMY24072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182744};
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 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 422 AA; 45793 MW; 3BA1BA5C9CA75A0E CRC64;
MARTVDAAET LKCSFCMKSQ RQVKKLITGS GVYICNECIE LCNEIIQEEL GDGEGKLAPS
KLPTPVEIFD FLNEYVIGQE EAKRTLSVAV YNHYKRLREL NKPKKQAQKN DVEIGKSNIL
LLGPTGTGKT YLAQSLARML DVPFAIADAT ALTEAGYVGE DVENVLLRLI QAAGDDVKRA
ESGIIYIDEI DKISRKSENP SITRDVSGEG VQQALLKIIE GTVASVPPQG GRKHPQGDYI
QIDTSNILFI CAGAFDGISQ IIAQRAGSGG IGFGARLHDV EAAPDQLADV TPDDLHRFGL
IPELVGRLPV IATVNALTEA DLIKILTEPK NALTKQYRKM FELDGVGLEF DDDALQAMAH
EAMERGTGAR GLRSIMERVL ASAMFEVPSR EDVSDVVVTR AAVLGEDDTE YILKGMASDK
TA
//