ID A0A0G3EED9_9BACT Unreviewed; 418 AA.
AC A0A0G3EED9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:AKJ64698.1};
GN ORFNames=L21SP4_01452 {ECO:0000313|EMBL:AKJ64698.1};
OS Kiritimatiella glycovorans.
OC Bacteria; Kiritimatiellota; Kiritimatiellia; Kiritimatiellales;
OC Kiritimatiellaceae; Kiritimatiella.
OX NCBI_TaxID=1307763 {ECO:0000313|EMBL:AKJ64698.1, ECO:0000313|Proteomes:UP000035268};
RN [1] {ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|Proteomes:UP000035268};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of the first cultured
RT representative of the subdivision 5 of the Verrucomicrobia phylum.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKJ64698.1, ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|EMBL:AKJ64698.1,
RC ECO:0000313|Proteomes:UP000035268};
RX PubMed=27300277; DOI=10.1038/ismej.2016.84;
RA Spring S., Bunk B., Sproer C., Schumann P., Rohde M., Tindall B.J.,
RA Klenk H.P.;
RT "Characterization of the first cultured representative of Verrucomicrobia
RT subdivision 5 indicates the proposal of a novel phylum.";
RL ISME J. 10:2801-2816(2016).
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}.
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DR EMBL; CP010904; AKJ64698.1; -; Genomic_DNA.
DR RefSeq; WP_052882001.1; NZ_CP010904.1.
DR AlphaFoldDB; A0A0G3EED9; -.
DR STRING; 1307763.L21SP4_01452; -.
DR KEGG; vbl:L21SP4_01452; -.
DR PATRIC; fig|1609981.3.peg.1508; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000035268; Chromosome.
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:AKJ64698.1};
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:AKJ64698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035268};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 1..50
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 9
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 12
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 31
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 34
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 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 418 AA; 46142 MW; DE36AD59A4ED3631 CRC64;
MTEDKPTRCS FCGKGEEEVD RLIAGPGVFI CSDCVELCEA VLQNEQAAEP GEGGEGTEQK
DAFSLMKPQE IKAALDEYVV GQEEAKRVLS VAVHNHYKRM LQRRRGGDGV ELEKSNILLA
GPTGCGKTLL ARTLANVLDV PYAVTDATTL TEAGYVGEDV ENILLTLLQA ADYNAERAQR
GIIYIDEIDK IGRRTENVSI TRDVSGEGVQ QALLKMLEGT TARIPPKGGR KHPHQEYIKL
DTTNILFICG GAFVGIDDII RRRSQDRSIG FTSGASADGA WKPASMRIEP EDLIKYGLIP
EFVGRIPVTT LLHPLREEEL VRILTEPRNA MTRQYQHLLE MDHIDLEFSE DGLHALARQA
IRRNTGARGL RAILEHLMLD LMYEAPSRED LERIVIDGDV VEGRSNPLDG ASGERKSA
//
