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Database: UniProt
Entry: A0A4P8RIB8_9BACT
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Original site: A0A4P8RIB8_9BACT 
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
//
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