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Database: UniProt
Entry: B1ZYJ7_OPITP
LinkDB: B1ZYJ7_OPITP
Original site: B1ZYJ7_OPITP 
ID   B1ZYJ7_OPITP            Unreviewed;       872 AA.
AC   B1ZYJ7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Oter_1950 {ECO:0000313|EMBL:ACB75233.1};
OS   Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=452637 {ECO:0000313|EMBL:ACB75233.1, ECO:0000313|Proteomes:UP000007013};
RN   [1] {ECO:0000313|EMBL:ACB75233.1, ECO:0000313|Proteomes:UP000007013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / JCM 15787 / PB90-1
RC   {ECO:0000313|Proteomes:UP000007013};
RX   PubMed=21398538; DOI=10.1128/JB.00228-11;
RA   van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA   Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA   Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA   Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT   "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT   abundant inhabitant of rice paddy soil ecosystems.";
RL   J. Bacteriol. 193:2367-2368(2011).
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. {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP001032; ACB75233.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1ZYJ7; -.
DR   STRING; 452637.Oter_1950; -.
DR   KEGG; ote:Oter_1950; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_0; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000007013; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007013};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          86..113
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          409..496
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   872 AA;  97219 MW;  1C028A35E06C9205 CRC64;
     MDFAKLTQMS RQAVTEAQNV ARRLHHNEVD TWHLLSALLG QENGIVPGLL DKLAITPSAV
     QLAVERELER LPKVTGSVDT SKVYVTQAVN EALTRAEDEA GKLKDEYVSV EHLFLGLLEV
     GKPDALKKLF KSFGLDRAKV LKALQDVRGA QRVTTDNPEA TYQALEKYGI DLVAQARKGK
     MDPVIGRDEE IRRTIRILSR KTKNNPVLIG EPGVGKTAIV EGLAQRILRG DVPEGLKDKT
     IFALDMGALV AGAKYRGEFE ERLKAVLTEI KQSEGRVLLF IDELHLIVGA GKTEGAMDAG
     NLLKPMLARG ELHCIGATTL DEYRKHIEKD AALERRFQPV VVDQPSVEDA ISILRGLRER
     FELHHGVKIQ DNALVSAVTL SNRYISDRFL PDKAIDLVDE ACAMIRTEMD SMPQELDELT
     RRVLRLEIEE TALAKEKDEA SARRLESLRK ELAEAREKAK AIRMHWEKEK AAIGRTRKLR
     EEIEAARLEM EKAERAYDLN KVAELRHGKI PQMEAELKKL EQAGAGATLF KEEVSEEEIA
     EVVSKWSGVP VTRLVEGEKE KLLRLEEVLH QRVVGQDEAV TLVTEAILRA RSGIKDPRRP
     VGSFLFLGPT GVGKTELAKT LAETLFDSEA AMVRIDMSEY MEKHSVARMI GAPPGYVGYD
     EGGQLTEAVR RKPYAVVLFD EIEKAHPDVF NVLLQVLDDG RITDSQGRTV DFKNTVIIMT
     SNIGSRYLLE GVSGSSIPDS VRESVMAELR KSFRPEFLNR IDETILFKPL TLEEITTIVD
     LLLADLNKRL ADRRVTVSLD AKAKEWTAEK GYDPVFGARP LKRFLQRNIE TKLARALISG
     EVGEDSAVKF TIKNDELVMA GKSSPIPAAA QR
//
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