ID   F1WU71_MORCA            Unreviewed;       858 AA.
AC   F1WU71;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   03-APR-2013, entry version 12.
DE   SubName: Full=ATP-dependent chaperone ClpB;
GN   ORFNames=E9Q_05079;
OS   Moraxella catarrhalis BC1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Moraxella.
OX   NCBI_TaxID=857576;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BC1;
RX   PubMed=21269504; DOI=10.1186/1471-2164-12-70;
RA   Davie J.J., Earl J., de Vries S.P., Ahmed A., Hu F.Z., Bootsma H.J.,
RA   Stol K., Hermans P.W., Wadowsky R.M., Ehrlich G.D., Hays J.P.,
RA   Campagnari A.A.;
RT   "Comparative analysis and supragenome modeling of twelve Moraxella
RT   catarrhalis clinical isolates.";
RL   BMC Genomics 12:70-70(2011).
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the clpA/clpB family.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; AERH01000029; EGE17850.1; -; Genomic_DNA.
DR   EnsemblBacteria; EGE17850; EGE17850; E9Q_05079.
DR   PATRIC; 52992153; VBIMorCat160656_1018.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0016485; P:protein processing; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013093; ATPase_AAA-2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR018368; Chaperonin_ClpA/B_CS.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR001270; Chaprnin_ClpA/B.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004176; Clp_N.
DR   InterPro; IPR023150; Dbl_Clp-N.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Repeat.
SQ   SEQUENCE   858 AA;  95296 MW;  EA42A644C2E638C7 CRC64;
     MNFEKYTRTL QEVIRGAQQS SLGHYHTAIA PVHLLSAVAD NHTALSIIEA SGANLARLQD
     EIKTLLSYQA VINQPTGQVN LSPETIKVLQ ATENYAAKAG DEFVPIEWLI LALFENKSLN
     KAFVSSGVTA QNLQTIMKNI RGDEAVTNQN SEQNRQALDK YTINLTERAM AGKLDPVIGR
     DDEIRRTVQV LSRRTKNNPV LIGEAGVGKT AIVEGLAQRI VNGEVPESLR NKSVLSLDMG
     SLIAGAKYHG EFEERLKAVL NELAKQDGNI ILFIDELHTM VGAGKTSGAM DAGNMLKPAL
     ARGELRCVGA TTLDEYRQYI EKDPALERRF QKVLVDEPTV EDTIAILRGL KERYELHHGV
     KIMDSAIIAA AKMSHRYITD RQLPDKAIDL IDEAASRIKM ELDSKPESLD KLDRRIIQLK
     MQLEAVKNEE DAGAKSQVKS LEQQIDDAQK QYSELEEVWK AEKVGVEKSK QFQAKLDTAR
     ITLEKALREG DYARASQLQY GEIIALEKQL AEEQTDEPEH APKLLRNKVT DNEIAEVVSH
     ATGIPVAKML QGERNKLLAM EDVLHERVIG QNEAVAAVAN AVRRSRSGLS DPNKPSGSFL
     FLGPTGVGKT ELTKALANFL FDSEDAMVRI DMSEYMEKHS VSRLVGAPPG YVGYEEGGVL
     TEAVRRKPYS VVLFDEVEKA HPDVFNILLQ VLDDGRLTDS QGRVVNFKNT VIIMTSNLGS
     HAIHEMTDSS YEDIKTAVMA SVTGHFRPEF INRIDEIVVF HGLGADQMTG IAEIQLDRLR
     TRLKERELGL SVSDEAMNHL VSVGYDPVFG ARPLKRAIQQ EIENPLAQLL LSGEFTTGDT
     IFVEWLNDQF TFNKLRYS
//