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Database: UniProt
Entry: A0A5C8JLI4_9BACT
LinkDB: A0A5C8JLI4_9BACT
Original site: A0A5C8JLI4_9BACT 
ID   A0A5C8JLI4_9BACT        Unreviewed;       873 AA.
AC   A0A5C8JLI4;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   08-NOV-2023, entry version 13.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:TXK37484.1};
GN   ORFNames=FVR03_15245 {ECO:0000313|EMBL:TXK37484.1};
OS   Pontibacter qinzhouensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=2603253 {ECO:0000313|EMBL:TXK37484.1, ECO:0000313|Proteomes:UP000321926};
RN   [1] {ECO:0000313|EMBL:TXK37484.1, ECO:0000313|Proteomes:UP000321926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY10130 {ECO:0000313|EMBL:TXK37484.1,
RC   ECO:0000313|Proteomes:UP000321926};
RA   Shi S.;
RL   Submitted (AUG-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:TXK37484.1}.
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DR   EMBL; VRTY01000060; TXK37484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C8JLI4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000321926; 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: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:UP000321926};
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;  97813 MW;  DA016FA77B8659BE CRC64;
     MNFNNYTIKA QEAIQKASEI AGGNQQQAIE TGHILKAILE TDENVTNFLL QKLNVNGRIL
     HSKLDEIVAG YPKVTGGGGP YLANDTAAAL QKATSYLKEF GDEYVAIEHM LLGLLAGRDK
     IAGLMKDVGF NEKDLKKAIK ELRGGAKVTD QNAEAKYNSL KRYAKDLNEL ARSGKIDPVI
     GRDEEIRRVL QILSRRTKNN PVLLGEPGVG KTAIVEGLAQ RIVSGDVPEN LKSKTLMSLD
     MGLLVAGAKY KGEFEERLKA VIKEVIDAEG EIVLFIDEIH TLIGAGAGGE SAMDAANLLK
     PALARGELHA IGATTLKEYQ KYIEKDKALE RRFQAVMVDE PSVPDAISIL RGIKDKYELH
     HGVRIKDDAI ISAVELSSRY ISDRFLPDKA IDLMDEAAAK LRIEIDSLPV ELDEIQRRIM
     QLEIEREAIR RENDKDKESV LSKEIADLSG KRDDLKAKWQ NEKQIIEGLQ KEKENIEQYK
     LEAEQAERAG DYGRVAELRY GKIQEAEAHL KQLQEQVREM QGENPMLKEE VNAEDIAEVV
     AKWTGIPVSK MLQSDREKLL NLEQELGKRV AGQEEAIEAI SDAVRRSRAG MQDPKRPIGS
     FIFLGTTGVG KTELAKALAD YLFNDENAMA RIDMSEYQER HAVSRLIGAP PGYVGYDEGG
     QLTEAIRRKP YSVVLLDEIE KAHPDVFNIL LQVLDDGRLT DSKGRVVNFK NTIIIMTSNI
     GSHIIQSNFQ SMEEYNKEEV IERTKVEVFD LLKKSVRPEF LNRIDELVMF RPLSRGDIRK
     IVDIQFHHIQ QRLEEAGIEL VATDEVLDYL GDQGFDPQFG ARPLKRVLQR QILNELSKEI
     LSGRISKDSV VEAVLQNSKI QFVNVDIELP TDK
//
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