ID A0A4P8RIB8_9BACT Unreviewed; 873 AA.
AC A0A4P8RIB8;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:QCR23606.1};
GN ORFNames=C1N53_15470 {ECO:0000313|EMBL:QCR23606.1};
OS Pontibacter sp. SGAir0037.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=2571030 {ECO:0000313|EMBL:QCR23606.1, ECO:0000313|Proteomes:UP000303242};
RN [1] {ECO:0000313|EMBL:QCR23606.1, ECO:0000313|Proteomes:UP000303242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGAir0037 {ECO:0000313|EMBL:QCR23606.1,
RC ECO:0000313|Proteomes:UP000303242};
RA Schuster S.C.;
RT "The complete genome of bacterial strain SGAirxxxx.";
RL Submitted (MAR-2018) 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; CP028092; QCR23606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P8RIB8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000303242; Chromosome.
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:UP000303242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 873 AA; 97925 MW; 9700CCBC74CF2CC4 CRC64;
MNFNNYTIKA QEAIQKATEI AGGNQQQAIE TGHILKAILE TDENVTNFLL KKLNVNSNML
NSKLNEAVNA YPKVTGGGGP YLANDAATAL QKATSFLKEF GDEYVAIEHV LLGILAGRDK
VAGIMKDVGF NEKDLKKAIK ELRGGTKVTD QNAEAKYNSL KRYAKDLNEL ARAGKIDPVI
GRDDEIRRVL QILSRRTKNN PVLLGEPGVG KTAIVEGLAQ RIVAGDVPEN LKSKTLMSLD
MGLLVAGAKY KGEFEERLKA VIKEVIDAEG EIILFIDEIH TLIGAGAGGE SAMDAANLLK
PALARGELHA IGATTLKEYQ KYIEKDKALE RRFQAVMVDE PSVPDAISIL RGIKDKYELH
HGVRIKDDAI IASVELSNRY ISDRFLPDKA IDLMDEAAAK LRIEIDSLPV ELDEIQRRIM
QLEIEREAIR RENDRDKEAS LSKEIADLSG KRDDLKAKWQ NEKQIIEGLQ KEKENIEQYK
LEAEQAERAG DYGRVAELRY GKIQEAEAKV KQLQEQVREM QGENPMLKEE VNAEDIAEVV
AKWTGIPVSK MLQSDREKLL HLEQELGKRV AGQEEAIEAI SDAVRRSRAG MQDPRRPIGS
FIFLGTTGVG KTELAKALAD YLFNDDNAMV RIDMSEYQER HAVSRLIGAP PGYVGYDEGG
QLTEAIRRKP YSVVLLDEIE KAHPDVFNIL LQVLDDGRLT DSKGRVVNFK NTIIIMTSNI
GSHIIQSNFE QMDEFNKDEV IERTKDEVFD LLKKSVRPEF LNRIDELVMF RPLSRGDIRK
IVDIQFKHIQ QRLEETGIQL IATDEVLDYL GEQGFDPQFG ARPLKRVLQR QILNELSKDI
LANRISKDSV VEAVLLEGKI HFINVDIELP TEK
//