ID A0A1T4QHK5_9BACT Unreviewed; 867 AA.
AC A0A1T4QHK5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04488132_108139 {ECO:0000313|EMBL:SKA03215.1};
OS Sediminibacterium ginsengisoli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Sediminibacterium.
OX NCBI_TaxID=413434 {ECO:0000313|EMBL:SKA03215.1, ECO:0000313|Proteomes:UP000190888};
RN [1] {ECO:0000313|EMBL:SKA03215.1, ECO:0000313|Proteomes:UP000190888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22335 {ECO:0000313|EMBL:SKA03215.1,
RC ECO:0000313|Proteomes:UP000190888};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUWH01000008; SKA03215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4QHK5; -.
DR STRING; 413434.SAMN04488132_108139; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000190888; 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 78, MITOCHONDRIAL; 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:SKA03215.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SKA03215.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190888};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 398..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 97021 MW; 133DEAB2083B8EA0 CRC64;
MNLNNYTIKA QETIQAAQQV AFNNGNPAIE TEHLLKALLA DKDSPVEFLL KKNNVNPSFA
ESKADEAIAR LPKAQGAEPA QQLGRELNTA LLKANAALSE FKDEFITPEH LLLGLLRTND
ATAKTLKAAG LTENGLVTAI KDLRKGDSIK SQTQEAQINA LNKYAKNLNE MARQGKLDPV
IGRDEEIRRT LHILSRRSKN NPILVGEPGV GKTAIAEGLA MRIVNGDVPE NLKSKTIFAL
DMGQLIAGAK YKGEFEERLK GVVKEVAESD GELILFIDEI HTLVGAGGGE GAMDAANILK
PALARGELRA IGATTLNEYQ KYFEKDKALE RRFQKVMIEE PSVEDAVSIL RGLKDRYETH
HHVRIKDEAI IAAVELSSRY ITDRFLPDKA IDLIDESAAK LRLEMNSMPE ELDKLERQIR
QLEIEREAIK RENDDEKLKD LNIDISNLSV ERDTLKAKWR EEKEVVEKIQ NAKAGIEGLK
LEAEQAERNG EYGKVAEIRY GKMKEQEALI EEYTKQLDEL SKHSRRLMKE EVDAEDIAAS
IAKATGIPVA KMMQGEREKL LHLEEELHNR VVGQDEAISA VADAIRRSRA GLQDPKKPIG
SFIFLGTTGV GKTELAKALA EYLFDDESMM TRIDMSEYQE KHTVSRLVGA PPGYVGYDEG
GQLTEAVRRK PYSVVLLDEI EKAHPDVWNI LLQVLDDGRL TDNKGRVVNF KNTIIIMTSN
IGSHLIQDAF DNVDEKNVED ATDKAKTDVM NLLRQTIRPE FLNRVDEIIM FSPLLKKQIT
GIVKIQLDGL KKMVAQNGIE LEFSDYLLDF LSEQGYDPQF GARPLKRLIQ KQIVNSLSKR
ILAGDIDKTK KVLVDVFDGI VVFRNEE
//
