ID   Q11QF1_CYTH3            Unreviewed;       871 AA.
AC   Q11QF1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   11-NOV-2015, entry version 82.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:ABG60363.1};
GN   OrderedLocusNames=CHU_3123 {ECO:0000313|EMBL:ABG60363.1};
OS   Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Cytophaga.
OX   NCBI_TaxID=269798 {ECO:0000313|EMBL:ABG60363.1, ECO:0000313|Proteomes:UP000001822};
RN   [1] {ECO:0000313|EMBL:ABG60363.1, ECO:0000313|Proteomes:UP000001822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / NCIMB 9469 {ECO:0000313|Proteomes:UP000001822};
RX   PubMed=17400776; DOI=10.1128/AEM.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C.,
RA   Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P.,
RA   Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B.,
RA   Wilson D.B., McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity). {ECO:0000256|SAAS:SAAS00202340}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034,
CC       ECO:0000256|SAAS:SAAS00015813}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU362034}.
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DR   EMBL; CP000383; ABG60363.1; -; Genomic_DNA.
DR   RefSeq; WP_011586472.1; NC_008255.1.
DR   SMR; Q11QF1; 157-340.
DR   STRING; 269798.CHU_3123; -.
DR   EnsemblBacteria; ABG60363; ABG60363; CHU_3123.
DR   KEGG; chu:CHU_3123; -.
DR   PATRIC; 21597113; VBICytHut34013_3106.
DR   eggNOG; ENOG4105C2Z; Bacteria.
DR   eggNOG; COG0542; LUCA.
DR   HOGENOM; HOG000218211; -.
DR   KO; K03695; -.
DR   OMA; NEMGRIV; -.
DR   OrthoDB; EOG65F8SM; -.
DR   BioCyc; CHUT269798:GJ83-3116-MONOMER; -.
DR   Proteomes; UP000001822; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004176; Clp_N.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR023150; Dbl_Clp-N.
DR   InterPro; IPR027417; P-loop_NTPase.
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   SUPFAM; SSF52540; SSF52540; 2.
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 {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000256|SAAS:SAAS00216097};
KW   Chaperone {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000256|SAAS:SAAS00127789};
KW   Coiled coil {ECO:0000256|RuleBase:RU362034};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001822};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000256|SAAS:SAAS00016018};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000256|SAAS:SAAS00216107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001822};
KW   Repeat {ECO:0000256|SAAS:SAAS00005595};
KW   Stress response {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000313|EMBL:ABG60363.1}.
FT   COILED      410    449       {ECO:0000256|RuleBase:RU362034}.
SQ   SEQUENCE   871 AA;  97520 MW;  B94695954B10EAAD CRC64;
     MNINNYTIKG QEAFQKAMEI VAANEQQSIE SVHLLKGIIV ADENVVPFLF KKNNINPVTF
     NQTLDAVIKT YGKVSGGSPY LSNDATQVLN KATALSKEFG DEYISIEHML LALVSGKDKA
     ATLLKDAGLS EKGLRAAIQE LRGTSKVTDQ HAEGKYRSLE KYSKNLNDLA RSGKIDPVIG
     RDEEIRRVLQ ILSRRTKNNP ILLGEPGVGK TAIAEGLAQR IVSGDVPENL KSKQLISLDM
     GLLVAGAKYK GEFEERLKSV IKEVIDSDGE IVLFIDEIHT LIGAGGGEGA MDAANLLKPA
     LARGELHAIG ATTLKEYQKY IEKDKALERR FQAVIVDEPN TQDAISILRG IKEKYEVHHG
     IRIQDDAIIA AVELSQRYIS DRYLPDKAID LMDEASAKLR IELDSMPQEL DEILRRIMQL
     EIEREAIRRE NNKEKETILS RELAELNEQK SQIMAKWQEE KRVIDGLKQA KEDIDRYKME
     AEQAERNGDY GKVAEIRYGK IQESEKQLVE FNKQLQELKQ TLGSSMLKEE VTPEDIAEVV
     AKWTGIPVSK MLQSEREKLL HLEEELGKRV AGQAEAIEAI SDAVRRSRAG LQDPKRPIGS
     FIFLGTTGVG KTELAKALAD YLFNDDNAMV RIDMSEYQES HAVSRLVGAP PGYIGYEEGG
     QLTEAVRRKP YSVILLDEIE KAHPDVFNIL LQVLDEGRLT DNKGRVANFK NAIIIMTSNM
     GAHVIQENFD KLTAANEDQV VEETKNEVID LLRKTIRPEF LNRVDEIIMF RPLTRKEIRK
     IVGIQFSLIQ KRLEENGIKV EASTEVLDKL GELGFDPQFG ARPLKRVMQR LILNELSKEI
     LSGNIQKESV VGITLGEDGN LQFLNLDSVP L
//