ID A0A1I1LR17_9BACT Unreviewed; 869 AA.
AC A0A1I1LR17;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05421780_109100 {ECO:0000313|EMBL:SFC75677.1};
OS Flexibacter flexilis DSM 6793.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flexibacteraceae;
OC Flexibacter.
OX NCBI_TaxID=927664 {ECO:0000313|EMBL:SFC75677.1, ECO:0000313|Proteomes:UP000199514};
RN [1] {ECO:0000313|EMBL:SFC75677.1, ECO:0000313|Proteomes:UP000199514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6793 {ECO:0000313|EMBL:SFC75677.1,
RC ECO:0000313|Proteomes:UP000199514};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FOLE01000009; SFC75677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1LR17; -.
DR STRING; 927664.SAMN05421780_109100; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199514; 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:SFC75677.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFC75677.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199514};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..143
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 403..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 97591 MW; 98C61DB9FFD88283 CRC64;
MNFNNYTIKS QEAIQKATEI AASAGQQAIE TGHLLQAILV SDENMIAFLL KKLNINRNLL
ETKLGEALQS YARTDGSPYL ANDAAAALQK ATSFLKEFGD EYVAIEHILL GLLAGKDRIA
QAMKDAGFAE KELKLAIKEL RGNARVTDQH AEGKYKSLER YSKNLNELAK AGKIDPVIGR
DEEIRRVLQI LSRRTKNNPI LLGEPGVGKT AIVEGLAQRI VSGDVPENLK TKTLVSLDMG
LLVAGAKYKG EFEERLKTVI KEVTDSDGEI ILFIDEIHTL IGAGGGGESA MDAANLLKPA
LARGELHTIG ATTLKEYQKY VEKDKALERR FQAVMVDEPS VPDAISILRG IKEKYELHHG
VRIKDDAVIA AVELSHRYIS DRFLPDKAID LMDEAASKLR IEIDSMPEEL DEVQRKIMQL
EIEREAIRRE NDTEKEQTLS KEIAELTEVR NDLKAKWQNE KNVIEAIQRE KENIEKLKLE
ADQAERQGDY GKVAELRYGS IRDAEQRLEV LNKQVQEKQG ENAMLKEVVT AEDIAEVVAK
WTGIPVNKML QSDRDKLLNL EAELGKRVAG QDTAIEAIAD AVRRSRAGLQ DPKRPIGSFI
FLGTTGVGKT ELAKALAEYL FNDDNALVRI DMSEFQERHA VSRLIGAPPG YVGYDEGGQL
TEAVRRKPYS VVLLDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVANFKNT IIIMTSNIGA
HLIQENFSHL TETNEEDVVF ETREQVFELL KKTIRPEFLN RIDEIVMFKP LSRKEMRKIV
QIQFKQIQQR LAESGIRLES EPEVLDYLAE VGYDPQFGAR PLKRVLQRRI LNELSKEILS
GRVNKDSVVG IVLDDDKNIQ FVNLDKVEL
//
