GenomeNet

Database: UniProt
Entry: A0A239K5K4_9ACTN
LinkDB: A0A239K5K4_9ACTN
Original site: A0A239K5K4_9ACTN 
ID   A0A239K5K4_9ACTN        Unreviewed;       868 AA.
AC   A0A239K5K4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05216276_102568 {ECO:0000313|EMBL:SNT12434.1};
OS   Streptosporangium subroseum.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=106412 {ECO:0000313|EMBL:SNT12434.1, ECO:0000313|Proteomes:UP000198282};
RN   [1] {ECO:0000313|EMBL:SNT12434.1, ECO:0000313|Proteomes:UP000198282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNT12434.1,
RC   ECO:0000313|Proteomes:UP000198282};
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; FZOD01000025; SNT12434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239K5K4; -.
DR   OrthoDB; 3170949at2; -.
DR   Proteomes; UP000198282; 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:SNT12434.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNT12434.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198282};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          87..114
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          410..504
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   868 AA;  96887 MW;  DC132E9970D20E16 CRC64;
     MDLNQLTQKS QEALHDAQTK ALRFGHTEID GEHLLLALID QPEGLIPRLM LAADADPNRL
     REELEAELNR RPRVSGPGVE PGQVYVTQRL SRLLEAAKRE ADRLKDEYVS VEHLLIALIE
     EGSETAAGRL LHEAGLSRDT FLKALTSIRG NQRVTSAMPE VAYEALEKYG RDLVADAVAG
     KLDPVIGRDA EIRRVIQILS RKTKNNPVLV GDPGVGKTAI VEGLAQRIGN GDVPEGLKGK
     TVFSLDMGSL VAGAKYRGEF EERLKAVLNE VKAAEGRILL FVDEMHTVVG AGAAEGAMDA
     GNMLKPMLAR GELHMIGATT LGEYRKHIEK DAALERRFQP VMIDEPSVED AVSILRGLRE
     RLEVFHGVKI QDSALVAAVV LSHRYISDRF LPDKAIDLVD EACAMLRTEI DSMPAELDEL
     TRRVMRLEIE ETALAKEEDA ASGARLEELR RELSDLRAEA DAMRAQWEAE RQALRTVQAL
     RVEIEQVRAE AERAERDYDL NRAAELRHGR LPELERRLQT EEERLLSKQG VARLLREVVT
     DDEISMIVSR WTGIPVSRLQ EGEREKLLRL DEILHERVVG QDEAVQLVAD AVIRARSGIK
     DPRRPIGSFI FLGPTGVGKT ELARALAEAL FDTEDNMVRI DMSEYQERHT VSRLVGAPPG
     YVGYEEGGQL TEAVRRKPYS VVLFDEVEKA HSDVFNTLLQ VLDDGRLTDA QGRTVDFRNT
     VLIMTSNIGS VYLLEGVTPG GEIKQDAKQQ VMAELRSRFR PEFLNRVDDI VIFKPLTPDE
     IERIVGLMLG ELRARLDQRG IRLEITEDAL RYIAEQGYDP VYGARPLRRF IAREVETRIG
     RALITGEAQE GAVIRVGLAE GELVVTYE
//
DBGET integrated database retrieval system