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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//