ID A0A4R2R357_9PSEU Unreviewed; 861 AA.
AC A0A4R2R357;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EV191_1011183 {ECO:0000313|EMBL:TCP57230.1};
OS Tamaricihabitans halophyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Tamaricihabitans.
OX NCBI_TaxID=1262583 {ECO:0000313|EMBL:TCP57230.1, ECO:0000313|Proteomes:UP000294911};
RN [1] {ECO:0000313|EMBL:TCP57230.1, ECO:0000313|Proteomes:UP000294911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45765 {ECO:0000313|EMBL:TCP57230.1,
RC ECO:0000313|Proteomes:UP000294911};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-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:TCP57230.1}.
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DR EMBL; SLXQ01000001; TCP57230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2R357; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000294911; 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:TCP57230.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCP57230.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000294911};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 93550 MW; 0CE5435ADF49F49E CRC64;
MDAFNPTTKT QQAISSALQA ATMNGNPDVA PAHLLGALLA QSDGITAPLL SAVGADPEKV
RGELEPLAQT LPSATGATVS APQFSADAVR SLTHAQRLAT EMGDEYVAAE HVLVGLAAEG
GAVADLLRKH GATAEALREA FVKVRGSARV SSPDPEDTYQ ALEKYGVDLT QQARSGELDP
VIGRDSEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIAEGL AQRIVAGDVP ESLRNKRVVS
LDLGSMVAGA KYRGEFEERL KAVLKEITDS DGQVITFIDE LHTIVGAGAT GEGAMDAGNM
IKPMLARGEL RMVGATTLDE YRQRIEKDPA LERRFQQVLV GEPSVGDTVG ILRGLKERYE
VHHGVRITDS ALVAAASLSD RYISARFLPD KAIDLVDEAA SRLRMEIDSR PVEVDEVERA
VRRLEIEEMA LSKEEDDESR KRRAALRAEL AEKREELSAL TARWQNEKGS IDKIRDLKEQ
LEQVRGESDR AERDGDLGRA AELRYGRIPA LEKELESATE STEHEQVMLK EEVGADDVAD
VVAAWTGIPA GRLLEGETGK LLRMEEELGE RVIGQAEAVR VVSDAVRRAR TGVADPDRPT
GSFLFLGPTG VGKTELAKSL AAFLFDDERA MIRIDMSEYS EKHSVARLVG APPGYVGYDQ
GGQLTESVRR RPYSVVLLDE VEKAHPDVFD VLLQVLDDGR LTDGQGRTVD FRNTILVLTS
NLGSQSIADA ALDEQQRNDA VLRVVRQHFK PEFLNRLDDV VVFHALSTNE LVSIVDIQVA
KLAERLGERR LTLDVTPGAR EWLALNGFDP VYGARPLRRL VQSAIGDQLA KELLSGGVRD
GDTVRVDVAG DTTAALTVHR A
//