CLPX_ALBFT
ID CLPX_ALBFT Reviewed; 421 AA.
AC Q21Y66;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=Rfer_1555;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_00175}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
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DR EMBL; CP000267; ABD69287.1; -; Genomic_DNA.
DR RefSeq; WP_011463855.1; NC_007908.1.
DR AlphaFoldDB; Q21Y66; -.
DR SMR; Q21Y66; -.
DR STRING; 338969.Rfer_1555; -.
DR EnsemblBacteria; ABD69287; ABD69287; Rfer_1555.
DR KEGG; rfr:Rfer_1555; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_4; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 718259at2; -.
DR Proteomes; UP000008332; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 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 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; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..421
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_1000024632"
FT DOMAIN 3..56
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 421 AA; 46145 MW; 7D3776742572F9EE CRC64;
MAEKKGSSGE KTLYCSFCGK SQHEVKKLIA GPSVFVCDEC IDLCNEIIRD ELPPSTEARG
DSSELPTPLE IKTNLDNYVI GQEPAKRTLA VAVYNHYKRL RHQEKAKKDD VELAKSNILL
IGPTGSGKTL LAQTLARMLD VPFVMADATT LTEAGYVGED VENIVLKLLQ SCNYEVERAQ
RGIVYIDEID KISRKSDNPS ITRDVSGEGV QQALLKLIEG TMASVPPQGG RKHPNQDFVQ
VDTTNILFIC GGAFSGLEKV IDNRTQSSGM GFGATVKSKE QRSLTEVFKE VEPEDLIKFG
LIPELVGRMP VLATLAELSE DALVQILTEP KNALVKQYSK LLAMEGVDLE IRPSALKAIA
KKALARKTGA RGLRSILEQS LIDTMFDLPN TSNVDKVVVD ESTIDENKPP LLVYREVAKK
A