(data stored in ACNUC10821 zone)

SWISSPROT: C8U2C5_ECO10

ID   C8U2C5_ECO10            Unreviewed;       424 AA.
AC   C8U2C5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS01076755};
GN   Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175,
GN   ECO:0000313|EMBL:BAI29283.1};
GN   OrderedLocusNames=ECO103_0415 {ECO:0000313|EMBL:BAI29283.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29283.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29283.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease.
CC       It directs the protease to specific substrates. Can perform
CC       chaperone functions in the absence of ClpP. {ECO:0000256|HAMAP-
CC       Rule:MF_00175, ECO:0000256|SAAS:SAAS01076750}.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric
CC       ring that, in the presence of ATP, binds to fourteen ClpP subunits
CC       assembled into a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes.
CC       {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00561096}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
CC       {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS01090919}.
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DR   EMBL; AP010958; BAI29283.1; -; Genomic_DNA.
DR   RefSeq; WP_000130305.1; NC_013353.1.
DR   SMR; C8U2C5; -.
DR   EnsemblBacteria; BAI29283; BAI29283; ECO103_0415.
DR   KEGG; eoh:ECO103_0415; -.
DR   HOGENOM; HOG000010093; -.
DR   KO; K03544; -.
DR   OMA; DIMYDLP; -.
DR   BioCyc; ECOL585395:ECO103_RS02175-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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; 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; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2C5.
DR   SWISS-2DPAGE; C8U2C5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00089772};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00326717};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000313|EMBL:BAI29283.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00448062};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00089789};
KW   Protease {ECO:0000313|EMBL:BAI29283.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00448058};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00063417}.
FT   DOMAIN       12     51       zf-C4_ClpX. {ECO:0000259|SMART:SM00994}.
FT   DOMAIN      111    333       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      317    412       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
FT   ZN_FING      15     40       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00175}.
FT   NP_BIND     120    127       ATP. {ECO:0000256|HAMAP-Rule:MF_00175}.
SQ   SEQUENCE   424 AA;  46356 MW;  9DEF1B0786E42B6F CRC64;
     MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE EIKEVAPHRE
     RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR NGDTSNGVEL GKSNILLIGP
     TGSGKTLLAE TLARLLDVPF TMADATTLTE AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI
     VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT
     SKILFICGGA FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL
     IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF RDEALDAIAK
     KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE SVIDGQSKPL LIYGKPEAQQ
     ASGE
//

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