ID A0A061QF54_9PROT Unreviewed; 421 AA.
AC A0A061QF54;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, 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:GAK32933.1};
GN ORFNames=AQ1_00811 {ECO:0000313|EMBL:GAK32933.1};
OS alpha proteobacterium Q-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK32933.1, ECO:0000313|Proteomes:UP000027360};
RN [1] {ECO:0000313|EMBL:GAK32933.1, ECO:0000313|Proteomes:UP000027360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q-1 {ECO:0000313|EMBL:GAK32933.1,
RC ECO:0000313|Proteomes:UP000027360};
RX PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT "Iodide oxidation by a novel multicopper oxidase from the
RT alphaproteobacterium strain Q-1.";
RL Appl. Environ. Microbiol. 78:3941-3949(2012).
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:GAK32933.1}.
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DR EMBL; BAYV01000009; GAK32933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061QF54; -.
DR STRING; 1492281.AQ1_00811; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000027360; 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:GAK32933.1};
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:GAK32933.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 3..56
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 15
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 18
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 37
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 40
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 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 421 AA; 45790 MW; E60523C214157E1E CRC64;
MTKLSGGDSK NTLYCSFCGK SQHEVRKLIA GPTVFICDEC VELCTDIIRE ESKSGIAKSS
DGVPTPQEIL DVLNDYVIGQ PKAKRVLSVA VHNHYKRLNH AAKSSDVELS KSNILLVGPT
GCGKTLLAQT LARILDVPFT MADATTLTEA GYVGEDVENI ILKLLQSADY NVERAQRGIV
YIDEVDKISR KSDNPSITRD VSGEGVQQAL LKIMEGTVAS VPPQGGRKHP QQEFLQVDTT
NILFICGGAF AGLDRIVSSR MQGKSMGFGA KVSSPEDRSV GELLMHAEPE DLLKFGLIPE
FVGRVPVIAT LEDLDEDALI EILSTPKNAL LKQYQRLFEM EDVALTFTDD ACRSVAKRAI
ARKTGARGLR SIMEDILLET MFDLPSLEGV EEVVINGDVV TSGAKPLFIY AERRDEAGTS
A
//