ID A0A558AL06_9PSEU Unreviewed; 870 AA.
AC A0A558AL06;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TVT24947.1};
GN ORFNames=FNH06_03730 {ECO:0000313|EMBL:TVT24947.1};
OS Amycolatopsis acidiphila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=715473 {ECO:0000313|EMBL:TVT24947.1, ECO:0000313|Proteomes:UP000318578};
RN [1] {ECO:0000313|EMBL:TVT24947.1, ECO:0000313|Proteomes:UP000318578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30562 {ECO:0000313|EMBL:TVT24947.1,
RC ECO:0000313|Proteomes:UP000318578};
RA Duangmal K., Teo W.F.A., Lipun K.;
RT "New species of Amycolatopsis and Streptomyces.";
RL Submitted (JUL-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TVT24947.1}.
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DR EMBL; VJZA01000004; TVT24947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A558AL06; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000318578; 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: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:UP000318578};
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 870 AA; 96607 MW; 2017922A424B7B36 CRC64;
MDVNRLTQKS QEALQEAQAL ASRLGHAEVD GEHLLFALLD QPGGLVPRLF EQAGADPVAL
RAAVEQDLAR RPAVTGAGAQ PGQVYVSRRV ARLLESAKRE ADRLKDEYVS VEHLVLALLE
EGAAAQAGRR LAEHGVTRDA FLSALTGVRG NQRVTSATPE GAYEALEKYG RDLVAEARSG
KLDPVIGRDG EIRRVVQILS RKTKNNPVLI GDPGVGKTAI VEGLAQRIHS GDVPEGLRDK
TIFALDMGAL VAGAKYRGEF EERLKAVLGE VTAAEGGILL FIDELHTVVG AGAAEGAMDA
GNMLKPMLAR GELHMIGATT LDEYRKHIET DAALERRFQL VLVDEPDVAD TISILRGLRE
RFEVFHGVKI HDGALVAAAT LSHRYITDRF LPDKAIDLVD EACARLRTEI DSMPAELDEL
TRRVTRLEIE EAALSKETDE ASKARLDQLR KELADLRAEA DAKKAQWEAE RRSIKRVQEL
RRDLERVRHE AEEAERAYDL NRAAELRYGE LAELERKLAA EEQRLSARQG ENRLLPEVVT
EDEIAEVVAA WTGIPVSRLR EGEREKLLRL DEILRSRVIG QDEAVTLVAD AIIRARSGIR
DPRRPIGSFV FLGPTGVGKT ELAKSLAAAL FDTEESMVRL DMSEYQERHT VSRLVGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HPDVFNTLLQ VLDDGRITDS QGRTVDFRNT
IVIMTSNIGS EYLLEGATGD GEIKPEARDR VMAALRRHFR PEFLNRIDDI VLFKPLGIEQ
LARIVDLQFE ELRSRLAEQR IEAELTEPAR RLIAERGFDP VYGARPLRRY LSHDVETRIG
RALLRGEVRP GQRICLDVAD GELTLRFGPQ
//