ID A0A4V3Z682_9MICC Unreviewed; 871 AA.
AC A0A4V3Z682;
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 ECO:0000313|EMBL:THJ68449.1};
GN ORFNames=E8P82_00595 {ECO:0000313|EMBL:THJ68449.1};
OS Arthrobacter echini.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1529066 {ECO:0000313|EMBL:THJ68449.1, ECO:0000313|Proteomes:UP000305233};
RN [1] {ECO:0000313|EMBL:THJ68449.1, ECO:0000313|Proteomes:UP000305233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM23 {ECO:0000313|EMBL:THJ68449.1,
RC ECO:0000313|Proteomes:UP000305233};
RA Liu Q., Xin Y.-H.;
RL Submitted (APR-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:THJ68449.1}.
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DR EMBL; SSWH01000001; THJ68449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3Z682; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000305233; 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:UP000305233};
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 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 94633 MW; B8F8C5898F78EAD6 CRC64;
MDTNFTTKSR EVLSAAAMNA STAGNAQIDT AHFLKALMDQ REGIAVALLK AAGADPDTVS
VQASNAIKAL PASSGASVAQ PQFSRQALQV VNTAKQEADR LGDQFVSTEH LLLALAADDG
AAGGILRGLD LTREALAAAL PGVRGEGRVN SPDPENTFQA LEKFGTDLTE VARSGKLDPV
IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLRGKRLISL
DLGSMIAGAK YRGEFEERLK AVLEEIRASD GEVVTFIDEL HTVVGAGASE GSMDAGNMLK
PMLARGELRL IGATTLDEYR ENVEKDPALE RRFQQVYVGE PSVPDTIGIL RGLKQRYEAH
HKVSIADSAL VAAATLSHRY IPGRQLPDKA IDLVDEAASR LRMEIDSAPV EIDELRRSLE
RMRMEEMALS RERDEASVER LEALRAEMAD RQEELDGLNA RWESEKAGLN RVGELKASLD
DLRSQADRAQ REGDLETASR ILYGQIPGLE RELSEAQAAE EQTVNTPDLM VAEEVTANDI
AEVISAWTGI PAGRMLQGES QKLLEMEERI GSRLIGQRRA VTAVSDAVRR ARAGVSDPNR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YSEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDLLLQVLDD GRLTDGQGRT VDFRNVILVL
TSNLGSQFLV DPSLDDAAKR AAVMSAVNAN FRPEFLNRLD DVVIFDPLGL DELSRIVDLQ
VDQLAERLRD RRLELDVSAA ASEWLALTGF DPAYGARPLR RLVQREIGDR LAKGILSGDI
VEGDTVVVDR SEEDDAALDE TGLTVRAAGQ M
//