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Database: UniProt
Entry: I0I0I6_CALAS
LinkDB: I0I0I6_CALAS
Original site: I0I0I6_CALAS 
ID   I0I0I6_CALAS            Unreviewed;       864 AA.
AC   I0I0I6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:BAL98773.1};
GN   OrderedLocusNames=CLDAP_07340 {ECO:0000313|EMBL:BAL98773.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL98773.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAL98773.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 {ECO:0000313|EMBL:BAL98773.1};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; AP012337; BAL98773.1; -; Genomic_DNA.
DR   RefSeq; WP_014432014.1; NC_017079.1.
DR   AlphaFoldDB; I0I0I6; -.
DR   STRING; 926550.CLDAP_07340; -.
DR   KEGG; cap:CLDAP_07340; -.
DR   PATRIC; fig|926550.5.peg.775; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_0; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000007880; 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:UP000007880};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..540
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   864 AA;  97493 MW;  905605F2B29D0239 CRC64;
     MRFDKFTQKA QAAVLEAQSL AEQRRAATVE PEHLLYTLVH QEGGVVPSLL ARIGVDVESL
     DRSIEQALAA LPRAQGASVQ VGFSRALADI LTDAQQLAGN MKDEYTSTEH LLLAMLSSTH
     KVKQLLARHG IDYNAVIQAL AAVRGNQRIT SDNPEAQYEA LKKYGRDLTE EARKGKLDPV
     IGRDEEIRRV IQILSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVKGDVPS TLRDKQVVAL
     DMGALLAGAK YRGEFEERLK AVLQEIVKSE GRIILFIDEI HTLVGAGAAE GAMDAANMLK
     PMLARGELHA IGATTLDEYR KHIEKDAALE RRFQPVFVDE PSVEDTISIL RGLKERYEVH
     HGVRITDSAV IAAATLSHRY ITDRFLPDKA IDLIDEAASR LRMQIDSKPQ ELDEIDRQIM
     QLEIEREALK KEKDEVSRQR LEELEKELAE LREKSAQLTA RWQAEKEAIQ RVRSIKEQID
     QVRIEIEQAE RAYDLQKVAE LRYGKMRQLE AELAQANARV QELQKQGALL KEEVDAEEIA
     EVVSKWTGIP VSKLLESERE KLLRMEEYLH RRVVGQDEAV RAVANAIRRS RAGLQDPNRP
     IGSFIFLGPT GTGKTELARS LAEYLFDDER ALIRIDMSEY QERHTVARLI GAPPGYIGYD
     EGGQLTEAVR RRPYSVVLFD EIEKAHPEVF NVLLQVLDDG RLTDSQGRTV DFKNTVIIMT
     SNLGSQYILD VAEVDEEVER RVREVLRSHF RPEFLNRIDE IVVFHALKRE QLKEIIDIQL
     ERLRKLLADR RITIELTDAA KELLINEGYD PAFGARPLKR VIQHRIADPL ALEILQGKIQ
     DGDHVLVDAI GDRLTFTAVE VLTE
//
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