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Database: UniProt
Entry: A0A1I2JR94_9ACTN
LinkDB: A0A1I2JR94_9ACTN
Original site: A0A1I2JR94_9ACTN 
ID   A0A1I2JR94_9ACTN        Unreviewed;       861 AA.
AC   A0A1I2JR94;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05216574_11738 {ECO:0000313|EMBL:SFF56483.1};
OS   Blastococcus sp. DSM 46838.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1798228 {ECO:0000313|EMBL:SFF56483.1, ECO:0000313|Proteomes:UP000198589};
RN   [1] {ECO:0000313|Proteomes:UP000198589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46838 {ECO:0000313|Proteomes:UP000198589};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOND01000017; SFF56483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2JR94; -.
DR   STRING; 1798228.SAMN05216574_11738; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198589; Unassembled WGS sequence.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:SFF56483.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFF56483.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   861 AA;  93813 MW;  8CB4F03C8A26C670 CRC64;
     MESKLTTRSQ EAVAGAQRLA VARGQAALEP LHLLAALLEQ SDGIAGPLLT AVGADPVDVR
     AKADAALRRM PSVSGATVPA PSPSRELLRV INDAGEQASA LGDEYISTEH LLVGLAGSAG
     EAGDVLTGAG ATRETLLAAF RTVRGNRKVT TPDPEGTFQA LEKYAVDLTQ RARDGKIDPV
     IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRMVAGDVPE SLKGKRLMAL
     DLSSMVAGAK YRGEFEERLK AVLQEITDAE GQIVTFIDEL HTIVGAGATG DSAMDAGNMI
     KPMLARGELR MVGATTLDEF REHIEKDPAL ERRFQQVFVG EPSVEDTIGI LRGLKERYEV
     HHGVRITDTA IVAAATLSDR YVTARFLPDK AIDLVDEAAS RLRMEIDSRP VEVDEVERAV
     RRMEIEEMAL SKEDDPSSME RLAALREELA NRRQELAELT FRWQQDKTAI DRIQRIKEEL
     ESVRLEAERA ERDGDLARAA ELRYGRLPEL ERSLTSAEES VAGGDSMLKE EVGPDDIAEV
     VQAWTGIPAG RLLEGETAKL LRMEDELGRR VVGQTDAVRA VSDAVRRARS GVADPNRPTG
     SFLFLGPTGV GKTELAKALA EFLFDDERAM VRIDMSEYSE KHSVARLVGA PPGYVGYESG
     GQLTEAVRRR PYTVVLFDEV EKAHQDVFDV LLQVLDDGRL TDGQGRTVDF RNTILILTSN
     LGSQLIADQS VPEASRREAV MDVVRTHFKP EFLNRLDDVV VFRALGSEEL TGIVEIQVGV
     LARRLAARRL TLQVTEAAKE WLAINGFDPV YGARPLRRLV QSAIGDQLAR ALLSGDIRDG
     DEVVVDRPAD VADGGLSVTR G
//
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