ID A0A563EZQ2_9PSEU Unreviewed; 866 AA.
AC A0A563EZQ2;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-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:TWP53008.1};
GN ORFNames=FKR81_07900 {ECO:0000313|EMBL:TWP53008.1};
OS Lentzea tibetensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=2591470 {ECO:0000313|EMBL:TWP53008.1, ECO:0000313|Proteomes:UP000316639};
RN [1] {ECO:0000313|EMBL:TWP53008.1, ECO:0000313|Proteomes:UP000316639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.1311 {ECO:0000313|EMBL:TWP53008.1,
RC ECO:0000313|Proteomes:UP000316639};
RA Huang J.;
RT "Lentzea xizangensis sp. nov., isolated from Qinghai-Tibetan Plateau
RT Soils.";
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:TWP53008.1}.
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DR EMBL; VOBR01000004; TWP53008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A563EZQ2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000316639; 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:UP000316639};
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 866 AA; 94294 MW; 256483EF6B714AB9 CRC64;
MDAFNPTTKT QQAVSAAVQA ATVGGHPDVS SVHLLSALLA QTDGLTAPLL SAVGADPTLV
RKELEQLSRS LPSASGTTVS APQLSRDAAR VLSRAQELAT EMGDEYVSTE HLLAGLAQYG
GQVADLLRRH GATPEAIREA FVHVRGSGRV SSPDPEGTFR ALDKYGVDLT ERARKGELDP
VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRVVAGDVP ESLRGKKVVS
LDLGSMVAGA KYRGEFEERL KAVLKEITDS AGQVITFIDE LHTIVGAGAT GESAMDAGNM
IKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV GEPSVEDTVG ILRGLKERYE
VHHGVRITDA ALVAAATLSD RYITARFLPD KAIDLVDEAA SRLRMEIDSR PVEIDTVERA
VRRLEIEEMA LAKESDPASM QRLTALRQEL AEKRETLSGL TARWQNEKGS IDKVRVLKGQ
LESLRGESER AERDGDLGRA AELRYGRIPA LEKELEVATQ STQDDSVMLK EEVGPDDVAD
VVSAWTGIPA GRLLEGETVK LLRMEDELAR RVIGQAEAVR VVSDAVRRSR AGVADPDRPT
GSFLFLGPTG VGKTELAKAL AEFLFDDERA MIRIDMSEYS EKHSVARLLG APPGYVGYDQ
GGQLTESVRR RPYSVVLLDE VEKAHPDVFD VLLQVLDDGR LTDGQGRTVD FRNTILVLTS
NLGSLAIADP SLDELERRDA VMAVVQRHFK PEFLNRLDDV VVFHSLATEE LTSIVDIQIE
RLGKRLSARR LTLDVTPSAR DWLALNGFDP VYGARPLRRL VQSSIGDQLA KELLAGEVRD
GDTVRVDVLD DNSGLIVGAT RSPATP
//