ID A0A4R8M0B4_9BACT Unreviewed; 880 AA.
AC A0A4R8M0B4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C8D99_12823 {ECO:0000313|EMBL:TDY54252.1};
OS Aminivibrio pyruvatiphilus.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Aminivibrio.
OX NCBI_TaxID=1005740 {ECO:0000313|EMBL:TDY54252.1, ECO:0000313|Proteomes:UP000295066};
RN [1] {ECO:0000313|EMBL:TDY54252.1, ECO:0000313|Proteomes:UP000295066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25964 {ECO:0000313|EMBL:TDY54252.1,
RC ECO:0000313|Proteomes:UP000295066};
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:TDY54252.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SORI01000028; TDY54252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R8M0B4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000295066; 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:TDY54252.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TDY54252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295066};
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 REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 417..497
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 880 AA; 97420 MW; 9BB616DFDF43924E CRC64;
MDFAKLTKKS QEALSEAQNK AISYGHAETD GEHLLLALLE QPEGLISRIL SRTGADPSAL
AGRVEQDLSR RPRVTGPGVE PGKIRISPRL SRLLLKAEER ADRLKDEYVS VEHLFASFFD
EGRTTAAGRI LAEGGVTEEK FLTALTEVRG RARVCSDNPE STYEALEKYG RDLVAMARAG
KLDPVIGRDE EVRRVIRILS RKTKNNPVLI GDPGVGKTAI VEGLAGRIVN GDVPEGLRDR
SIFALDMGAL VAGAKFRGEF EERLKAVLNE VKESDGRIIL FIDELHTIVG AGAAEGAIDA
GNMLKPMLAR GELHCIGATT VDEFRKHIEK DAALARRFQP VLVEQPSVED AVSILRGLKD
RFQVHHGVKI RDNALVAAAV LSNRYITERF LPDKAIDLVD EACAMIRTEI DSLPAELDTV
SRKVMQLEIE EAALTKEKDS ASLGRLKNLR AELQEAREEQ VSLRAGYEAE KQGLAEVREL
REQIESVRRD IGKAEREYDL NRAAELKHGT LPQLEDRLRR KEEEIQARGQ GTRILREEVT
ENEISEIVSR WTGIPVNRLL EGEKEKLLRL GDILHRRVVG QDEAVDLVAD AVLRARAGIK
DPRRPIGSFI FLGPTGVGKT ELAKTLAEAL FDSEDNLVRL DMSEYMEKHS VSRMVGAPPG
YVGYDEGGQL TEAVRRKPYS VLLFDEIEKA HPDVFNILLQ ILDDGRITDS RGHVVNFKNT
VIIMTSNIGA PLLLQGITSE GEIRENARDG VMEELRRSFR PEFLNRVDDV VLFKPLTPAE
IGRIVRLLAS ALSDRLRERN ISLEITDRGA AFIAAAAYDP VYGARPLKRY MVRNIETPVA
RMIISGEAGE GTVIIVDEGE GKLVLRTAAS GEEDVQPNNS
//