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Database: UniProt
Entry: A0A1H6EFB9_9ACTN
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ID   A0A1H6EFB9_9ACTN        Unreviewed;       874 AA.
AC   A0A1H6EFB9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05216223_13450 {ECO:0000313|EMBL:SEG95709.1};
OS   Actinacidiphila yanglinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310779 {ECO:0000313|EMBL:SEG95709.1, ECO:0000313|Proteomes:UP000236754};
RN   [1] {ECO:0000313|EMBL:SEG95709.1, ECO:0000313|Proteomes:UP000236754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2023 {ECO:0000313|EMBL:SEG95709.1,
RC   ECO:0000313|Proteomes:UP000236754};
RA   de Groot N.N.;
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; FNVU01000034; SEG95709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6EFB9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000236754; 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:SEG95709.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEG95709.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236754};
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          403..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   874 AA;  96895 MW;  C021F9687BC3736F CRC64;
     MDMNRLTQKS QEALQEAQSV AVRMGQTEVD GEHLLLALLD QQDGLTTRLL ADTGADPAAL
     RAAVEADLAK RPRTTGPGAT PGQVMVTQRL ARLLDTAEQE AKRLKDEYVS TEHLVLALVN
     EGSTTAAGRR LGEQGVSKDS FLAALTTVRG NQRVTSANPE EAYEALDKYG RDLVVEARTG
     RLDPVIGRDA EIRRVIQILS RKSKNNPVLI GEPGVGKTAI VEGLAQRIVR GDVPEGLRDK
     TVFSLDMGSL VAGAKYRGEF EERLKAVLSE VKGAEGRILL FVDELHTVVG AGAAEGAMDA
     GNMLKPMLAR GELHMIGATT LDEYRKHIES DAALERRFQT VLVDEPSVED AVSILRGIRE
     RLEIFHGVKI QDNALVAAAT LSHRYISDRF LPDKAIDLVD EACARLRTEI DSMPAELDEL
     TRRATRLEIE EAALDQETDP ASRARLEDLR HELADLRGEV DAKHAQWEAE RQAIRKVQEL
     RQELERARQE AEEAERAYDL NRAAQLRYGT VSELERRLAA EEEQLAAKQG ETRLLREVVT
     ADEIAEIVSA WTGIPVTRLQ EGERQKLLKL DEILRERVVG QDEAVQLVAD AVIRARSGVR
     DPRRPIGSFI FLGPTGVGKT ELAKTLAAAL FDSETNMIRL DMSEYQERHT VSRLVGAPPG
     YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HADVFNTLLQ VLDDGRITDA QGRTVDFRNT
     VIIMTSNLGS QYLLQDATHA GEIKPEARAL VMTELNGHFR PEFLNRVDDI VLFHPLGIAQ
     IERIVDLLLD ELRDRLSEQR ITLVLTEPAR HLIAAEGYDP VYGARPLRRF ISHEVETRIG
     RALLSGEARE GVTILVDAED GQLIVTLQDE PQEP
//
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