(data stored in ACNUC7421 zone)

SWISSPROT: CLPX_ECODH

ID   CLPX_ECODH              Reviewed;         424 AA.
AC   B1XFM6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 65.
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=ECDH10B_0394;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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:0000255|HAMAP-
CC       Rule:MF_00175}.
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:0000255|HAMAP-Rule:MF_00175}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
CC       {ECO:0000255|HAMAP-Rule:MF_00175}.
DR   EMBL; CP000948; ACB01566.1; -; Genomic_DNA.
DR   RefSeq; WP_000130305.1; NC_010473.1.
DR   ProteinModelPortal; B1XFM6; -.
DR   SMR; B1XFM6; -.
DR   EnsemblBacteria; ACB01566; ACB01566; ECDH10B_0394.
DR   KEGG; ecd:ECDH10B_0394; -.
DR   eggNOG; ENOG4105CHN; Bacteria.
DR   eggNOG; COG1219; LUCA.
DR   HOGENOM; HOG000010093; -.
DR   KO; K03544; -.
DR   OMA; DIMYDLP; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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   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; B1XFM6.
DR   SWISS-2DPAGE; B1XFM6.
KW   ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    424       ATP-dependent Clp protease ATP-binding
FT                                subunit ClpX.
FT                                /FTId=PRO_1000097952.
FT   ZN_FING      15     40       C4-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00175}.
FT   NP_BIND     120    127       ATP. {ECO:0000255|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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