ID A0A4Q7NUT5_9ACTN Unreviewed; 869 AA.
AC A0A4Q7NUT5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EV189_0217 {ECO:0000313|EMBL:RZS90986.1};
OS Motilibacter rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Motilibacterales;
OC Motilibacteraceae; Motilibacter.
OX NCBI_TaxID=598652 {ECO:0000313|EMBL:RZS90986.1, ECO:0000313|Proteomes:UP000293638};
RN [1] {ECO:0000313|EMBL:RZS90986.1, ECO:0000313|Proteomes:UP000293638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45622 {ECO:0000313|EMBL:RZS90986.1,
RC ECO:0000313|Proteomes:UP000293638};
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 (FEB-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:RZS90986.1}.
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DR EMBL; SGXD01000001; RZS90986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q7NUT5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000293638; 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:RZS90986.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RZS90986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000293638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 94009 MW; D4F6C68F23294118 CRC64;
MDTSSFTTRS EEALADAVRR ASAAGSAQVE PVHVLLALLA QDGTVVPPLL TAVGADPGTV
RARAEQLAAR IPSASGSSVA APQISRPTYD ALSSAGEAAR HLGDTFVSTE HLLVGLARSG
GEVATLLTTL GATPEGLLDG FAGVRGATKV SSKDPEATYQ ALEKYGVDLT ARARGGELDP
VIGRDSEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP ESLKGKKLVA
LDLAAMVAGA KYRGEFEERL KAVLAEIQQS EGQVVTFIDE LHTVVGAGAG GEGAMDAGNM
LKPMLARGEL RLVGATTLDE YREHIEKDPA LERRFQQVLV GEPSVEDTIG ILRGLRGRYE
AHHKVAISDA ALVAAATLSD RYITSRFLPD KAIDLVDEAG SRLRMEIDSK PVEIDELQRA
VDRLRMEEMA LEREDDPASQ ERLAALRKRL ADDNERLTAL NLRWEQEKSG LNKVGALKER
LDDLRGQAER AQRDGDFESA SRLMYAEIPA LERDLAAAQD AERHTDVMVK EEVGPDDVAD
VVAAWTGIPA GRLLEGETAK LLRMEEELGR RLIGQRQAVQ AVSDAVRRAR AGISDPNRPT
GSFLFLGPTG VGKTELAKAL ADFLFDDERA MVRIDMSEYA EKHSVSRLVG APPGYVGYEE
GGQLTEAVRR RPYSVVLLDE VEKAHPEVFD VLLQVLDDGR LTDGQGRTVD FRNVILVLTS
NLGSVYLVDS TMSEEAKREA VMGVVRGTFR PEFLNRLDEV VVFDALGTEE LGRIVELQIA
ALQRRLDGRR LTLDVTPAAR DWLALSGFDP VYGARPLRRL VQKEIGDNLA RALLGGDVRD
GDTVRIDVDV PGNRLTVAAE RPLAVERTG
//