CLPX_CLOBH
ID CLPX_CLOBH Reviewed; 429 AA.
AC A5I6W0; A7G845;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
GN OrderedLocusNames=CBO3230, CLC_3141;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000727; ABS36889.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL84792.1; -; Genomic_DNA.
DR RefSeq; WP_003357457.1; NC_009698.1.
DR RefSeq; YP_001255720.1; NC_009495.1.
DR RefSeq; YP_001388960.1; NC_009698.1.
DR AlphaFoldDB; A5I6W0; -.
DR SMR; A5I6W0; -.
DR GeneID; 5187485; -.
DR KEGG; cbh:CLC_3141; -.
DR KEGG; cbo:CBO3230; -.
DR PATRIC; fig|413999.7.peg.3209; -.
DR HOGENOM; CLU_014218_8_2_9; -.
DR OMA; HYKRVQA; -.
DR PRO; PR:A5I6W0; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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 GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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..429
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_1000058334"
FT DOMAIN 1..53
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT REGION 408..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 34
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 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 429 AA; 47859 MW; B83D221EC13D39C9 CRC64;
MSKLDEKKQL KCSFCGKTQD QVRRLIAGPG VYICDECIEL CSEIINDEFE DDIQVDLTSL
PKPTEIKTYL DQYVIGQEDA KKSLSVAVYN HYKRINSNTN NDDVELQKSN ILLLGPTGSG
KTLLAQTLAK FLNVPFAIAD ATTLTEAGYV GEDVENILLK LIQNADYDIE KAEKGIVYID
EIDKIARKSE NPSITRDVSG EGVQQALLKI LEGTVAAVPP QGGRKHPHQE FIQINTTNIL
FICGGAFDGV DKIIERRTRT SSLGFGAEIQ SKKEKDLGKL LKDIMPGDLL KFGLIPEFIG
RLPIVVTLDK LDREALIKIL TEPKNALVKQ YKKLFELDDV ELEFNQEALK EIADEAINRN
TGARGLRAII EDMMREIMFD IPSQENIGKV IVNEDCIKTK KPELIEAEGG KRLPIKPKKG
KKRKDSETA
