CLPX_RHIWR
ID CLPX_RHIWR Reviewed; 424 AA.
AC A5V3U4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Swit_0592;
OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=392499;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA Richardson P.;
RT "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL Submitted (MAY-2007) 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; CP000699; ABQ66960.1; -; Genomic_DNA.
DR RefSeq; WP_011951440.1; NC_009511.1.
DR AlphaFoldDB; A5V3U4; -.
DR SMR; A5V3U4; -.
DR STRING; 392499.Swit_0592; -.
DR EnsemblBacteria; ABQ66960; ABQ66960; Swit_0592.
DR KEGG; swi:Swit_0592; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_5; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 718259at2; -.
DR Proteomes; UP000001989; 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..424
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_1000024669"
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 120..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 424 AA; 46025 MW; 27D394E60BE6B933 CRC64;
MTKLTGGDSK STLYCSFCGK SQHEVRKLIA GPTVFICDEC VELCNDIIRE ETKGALVSKK
DGGVPTPHEI CEHLDQYVIG QAKAKRVLSV AVHNHYKRLN HGAKGADVEL AKSNILLVGP
TGSGKTLLAQ TMARLLDVPF TMADATTLTE AGYVGEDVEN IILKLLQASD YNVERAQRGI
VYIDEIDKIS RKADNPSITR DVSGEGVQQA LLKLMEGTTA SVPPQGGRKH PQQEFLQVDT
TNILFICGGA FAGLEKIIGD RLQGKSIGFG AYVAAPEERR TGETLQQCEP EDLLKFGLIP
EFVGRLPVIA TLMDLDEAAL VEILTAPKNA LVKQYQKLFD MEGVKLGFTD DALVAIARKA
ITRKTGARGL RSILEGLLLD TMFDLPSMDG VDEIMVDKDV VEGRKDPVRV FTKKNKEKAG
GDAA