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Database: UniProt
Entry: A0A1H7QK32_9BURK
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ID   A0A1H7QK32_9BURK        Unreviewed;       865 AA.
AC   A0A1H7QK32;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05216319_1887 {ECO:0000313|EMBL:SEL47627.1};
OS   Duganella sp. CF402.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1855289 {ECO:0000313|EMBL:SEL47627.1, ECO:0000313|Proteomes:UP000198529};
RN   [1] {ECO:0000313|Proteomes:UP000198529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF402 {ECO:0000313|Proteomes:UP000198529};
RA   Varghese N., Submissions S.;
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. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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; FOBG01000001; SEL47627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7QK32; -.
DR   STRING; 1855289.SAMN05216319_1887; -.
DR   Proteomes; UP000198529; 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 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   Hydrolase {ECO:0000313|EMBL:SEL47627.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEL47627.1};
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          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   865 AA;  95753 MW;  2E6CCF2F7BA107F6 CRC64;
     MRQDKLTTKL QEALSDSQSL AVGNDNQYIE PVHLLTALLN QDDGSARSLL QRAGVNVGGL
     TKALTAALER LPKVSGTDGN VQASRELVGV LNMADKEAQK RVDQFISSEM VLLALTDDKS
     EAGKLAREAG LTRKSLEAAI DTVRGGAKVD SQEAEGQREA LKKYTLDLTE RARLGKLDPV
     IGRDDEIRRA IQVLQRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNNEVPD SLKGKRVLAL
     DMAALIAGAK YRGEFEERLK SVLKELAMDE GQTIVFIDEM HTMVGAGKAD GAMDAGNMLK
     PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKILVDE PTVEATIAIL RGLQDKYELH
     HKVAISDAAI IAAAELSHRY ITDRFLPDKA IDLIDEAAAK IKIEIDSKPE VMDKLERRLI
     QLKIEKEAVK KEKDEGSRKR LELIDEEIER LTRELNDFEE ILKAEKAVVQ GSTHIKEEIE
     QIKQQMEQAT RESNWQRVSE LQYGRLPQLE AELKLAEAAS AKGVSLEKDT PPKQRLLRTE
     VGSEEIAEVV SRATGIPVSR MMQGEREKLL HIEDKLHERV VGQDEAISAV ADAIRRSRAG
     LADPNRPYGS FLFLGPTGVG KTELTKALAG FLFDTEESLI RIDMSEFMEK HSVARLIGAP
     PGYVGYDEGG YLTEAVRRKP YSVILLDEVE KAHPDVFNVL LQALDDGRMT DGQGRTVDFK
     NTVIIMTSNL GSHKIQSMED SDPGVVKLAV MAEVRSHFRP EFINRIDEIV VFHGLDEKNI
     GAIARIQLVT LQQRLAKLEI GLEVSEDALH KIAEAGYDPV YGARPLKRAI QQQIENPLSK
     LILQGKFGPK DTIHVDVASG ELAFR
//
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