GenomeNet

Database: UniProt
Entry: A0A239G5E0_9ACTN
LinkDB: A0A239G5E0_9ACTN
Original site: A0A239G5E0_9ACTN 
ID   A0A239G5E0_9ACTN        Unreviewed;       865 AA.
AC   A0A239G5E0;
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=SAMN06265355_12326 {ECO:0000313|EMBL:SNS64321.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS64321.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNS64321.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS64321.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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; FZNP01000023; SNS64321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239G5E0; -.
DR   OrthoDB; 3170949at2; -.
DR   Proteomes; UP000198420; 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:SNS64321.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNS64321.1};
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          84..111
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          412..529
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   865 AA;  95250 MW;  7E13FBBCC5E1283C CRC64;
     MDYKLTQKSQ EALSVAVRRA AAEGHPEVEP QHLLVALIGL PDGTAVPLLE AVGADWQVVR
     RRAEEQLAAM PKAQGSTVAT PRLSGQLQRS VNTAANRAQQ LEDEYVSTEH LLVGLAADGG
     PAAGLLKEFG AAPEALLEAF EKVRGHARVT SENPEGTYQS LEKYGVDLTA AARDGRLDPV
     IGRDPEIRRV IQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIIAGDVPE SLRGKRLVSL
     DLGAMVAGAK YRGEFEERLK AVLNEIKKSE GQVVTFIDEL HTVVGAGAAE GAMDAGNMLK
     PMLARGELRM IGATTLDEYR ERIEKDAALE RRFQQVFVGE PTVEDTIAIL RGLKGRYEAH
     HKVQINDSAM VAAATLSDRY ITSRFLPDKA IDLVDEAASR LRMEIDSRPV EVDELQRAVD
     RLKMEQMNLE KETDEASRQR LERLRADLAD RQEQLSGVNA RWEREKAELN RVGEIKERID
     QLRGEAARAE RDGDLETSSR LVYGEIPALE KQLEEAAEAT ETRDTMVKEE VGPDDVADVV
     ASWTGIPAGR LLEGETAKLL RMEDDLGRRL IGQEAAVRTV SDAVRRARAG ISDPDRPTGS
     FLFLGPTGVG KTELAKALAE FLFDDERAMT RIDMSEYSEK HSVARLVGAP PGYIGYEEGG
     QLTEAVRRRP YSAVLLDEVE KAHPEVFDIL LQVLDDGRLT DGQGRTVDFR NTILILTSNI
     GSQFLVDPTL ENGAKREAVW NAVRNSFKPE FLNRLDDVIL FDALSTEELT RIVDLQVDRL
     ADRLADRQLA LRVTPAAREW LALTGYDPLY GARPLRRLVQ TAIGDQLARE LLSGEVRDGD
     EVVVDLDEAA DRLTVERSGG LNLTK
//
DBGET integrated database retrieval system