ID V8CBD6_9HELI Unreviewed; 455 AA.
AC V8CBD6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ORFNames=HMPREF2086_00056 {ECO:0000313|EMBL:ETD24723.1};
OS Helicobacter macacae MIT 99-5501.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1357400 {ECO:0000313|EMBL:ETD24723.1, ECO:0000313|Proteomes:UP000018731};
RN [1] {ECO:0000313|EMBL:ETD24723.1, ECO:0000313|Proteomes:UP000018731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 99-5501 {ECO:0000313|EMBL:ETD24723.1,
RC ECO:0000313|Proteomes:UP000018731};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
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}.
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:ETD24723.1}.
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; AZJI01000001; ETD24723.1; -; Genomic_DNA.
DR RefSeq; WP_023926725.1; NZ_KI669454.1.
DR AlphaFoldDB; V8CBD6; -.
DR STRING; 1357400.HMPREF2086_00056; -.
DR PATRIC; fig|1357400.3.peg.81; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_7; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000018731; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein 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; 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 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 SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000313|EMBL:ETD24723.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW Hydrolase {ECO:0000313|EMBL:ETD24723.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW Protease {ECO:0000313|EMBL:ETD24723.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018731};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 146..308
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 348..442
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 119..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 455 AA; 50391 MW; E36C089E0507DDF6 CRC64;
MNQPICNFCG NSITPHRQGL RAKYPNPNDP NSSFAFICLP CISSVYKEFL DPIYGVKKST
LSTQKQSLNL DLPSSRVPSP KELKAKLDEY VIGQEEAKKV FCVAIYNHYK RIANNLAQAK
QDSEQNQASS FDSSDKGSSS DDVEIAKSNI LLIGPTGSGK TLMAQTLARF LDVPIAISDA
TSLTEAGYVG EDVENILTRL YQAADGDIEK TQRGIVFIDE IDKISRLSEN RSITRDVSGE
GVQQALLKII EGSVVNISEK GGRKHPNERF VQIDTTNILF ICGGAFDGLS EIIQRRMGDN
VLGFGQVQKT KSQQKDVLNL VEPDDLVSYG LIPELIGRLH ITATLQPITK EAMIDILTKP
KNALIKQYQK LFEVDDNVKL SFEKEAIESI AELAIARKTG ARGLRAIIEE FMTDIMFDLP
SMREHEVVIT KDCVEQKSKP LLIKHKKISN KVKGA
//
