(data stored in ACNUC7421 zone)

SWISSPROT: CLPX_HISS2

ID   CLPX_HISS2              Reviewed;         414 AA.
AC   B0UW19;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 72.
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=HSM_0214;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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}.
DR   EMBL; CP000947; ACA31837.1; -; Genomic_DNA.
DR   RefSeq; WP_012341085.1; NC_010519.1.
DR   SMR; B0UW19; -.
DR   PRIDE; B0UW19; -.
DR   EnsemblBacteria; ACA31837; ACA31837; HSM_0214.
DR   GeneID; 31486493; -.
DR   KEGG; hsm:HSM_0214; -.
DR   HOGENOM; HOG000010093; -.
DR   KO; K03544; -.
DR   OMA; HYKRVQA; -.
DR   OrthoDB; 718259at2; -.
DR   BioCyc; HSOM228400:G1GB8-220-MONOMER; -.
DR   Proteomes; UP000008543; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.50.30; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   InterPro; IPR038366; Znf_CppX_C4_sf.
DR   PANTHER; PTHR11262; PTHR11262; 2.
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;
DR   PRODOM; B0UW19.
DR   SWISS-2DPAGE; B0UW19.
KW   ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..414
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_1000077161"
FT   DOMAIN          1..50
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   NP_BIND         118..125
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
FT   METAL           9
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   METAL           12
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   METAL           31
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   METAL           34
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
SQ   SEQUENCE   414 AA;  46070 MW;  5C9578E541A08F9E CRC64;
     MTKEKELHCS FCGKEQKEVD KLIAGTSGYI CNECIELCHD MLANADDIEE IDEEFQEEEP
     KLPTPHEIRA HLDDYVIGQD YAKKVLAVAV YNHYKRLRSE KNTSEVELGK SNILLIGPTG
     SGKTLLAQTL ARMLNVPFAM ADATTLTEAG YVGEDVENVL QKLLQNCDYD IEKAQQGIIY
     IDEIDKITRK SENPSITRDV SGEGVQQALL KLVEGTVASI PPQGGRKHPQ QEMLRVDTSK
     ILFICGGAFA GLDKIIEKRT NTSGKGIGFG ADVRIDEEKV SLTELFKQVE PDDLMKFGLI
     PEFIGRLPVI APLSELDEEA LVKILTEPKN ALTKQYQVLF SLENIELEFT QEALIAMAKK
     ALARKTGARG LRSIVETLLL DTMYDLPSIE NLQKVIVEEE TVTENKVPVL KFNS
//

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