ID A0A3N4D1K8_9ACTN Unreviewed; 427 AA.
AC A0A3N4D1K8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:VEJ58883.1};
GN ORFNames=FBF34_08860 {ECO:0000313|EMBL:QCT38065.1}, NCTC11666_01753
GN {ECO:0000313|EMBL:VEJ58883.1}, NCTC12967_01783
GN {ECO:0000313|EMBL:VEH70486.1};
OS Arachnia propionica.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Arachnia.
OX NCBI_TaxID=1750 {ECO:0000313|EMBL:VEJ58883.1, ECO:0000313|Proteomes:UP000278659};
RN [1] {ECO:0000313|Proteomes:UP000273044, ECO:0000313|Proteomes:UP000278659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11666 {ECO:0000313|EMBL:VEJ58883.1,
RC ECO:0000313|Proteomes:UP000278659}, and NCTC12967
RC {ECO:0000313|EMBL:VEH70486.1, ECO:0000313|Proteomes:UP000273044};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCT38065.1, ECO:0000313|Proteomes:UP000309405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0700 {ECO:0000313|EMBL:QCT38065.1,
RC ECO:0000313|Proteomes:UP000309405};
RA Collins A.J., Murugkar P., Chen T., Dewhirst F.E.;
RT "Saccharibacteria TM7 and host bacteria genomes.";
RL Submitted (APR-2019) 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}.
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DR EMBL; CP040007; QCT38065.1; -; Genomic_DNA.
DR EMBL; LR134406; VEH70486.1; -; Genomic_DNA.
DR EMBL; LR134535; VEJ58883.1; -; Genomic_DNA.
DR RefSeq; WP_014846844.1; NZ_RKKA01000001.1.
DR AlphaFoldDB; A0A3N4D1K8; -.
DR GeneID; 64407240; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000273044; Chromosome 1.
DR Proteomes; UP000278659; Chromosome 1.
DR Proteomes; UP000309405; 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:VEJ58883.1};
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:VEJ58883.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273044};
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 126..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 427 AA; 47020 MW; 395A0416EA7ADCF2 CRC64;
MPRIGETSEV FKCNFCTKSQ KQVKRLIAGD GVYICDECIG LCNEIIEEEF PRVETFGLQE
ELPKPKEIRD FLDQYVIGQD AAKKALAVAV YNHYKRITSE QTRIGRSRQG EEPVEVGKSN
ILLIGPTGCG KTYLAQTLAK MLNVPFAMAD ATALTEAGYV GEDVENILLK LIQAADFDIK
KAETGIIYID EIDKVARKSE NPSITRDVSG EGVQQALLKI LEGTVASVPP QGGRKHPHQD
FLQIDTTKVL FIVGGAFAGL DEIINSRIGK RPLGFSVDTS ARKEVTDPFS EVRPEDLHKF
GLIPEFIGRL PMISTVSPLD REALNRILVE PRNALTKQFA RLFELDGVQL DFTDEAIDAI
AELALERGTG ARGLRAILEE LLLDVMFEVP SAEDVAQVVV TREAVLGKAQ PELVASSRVA
RRRDLSA
//