GenomeNet

Database: UniProt
Entry: A0A317EAR8_9PROT
LinkDB: A0A317EAR8_9PROT
Original site: A0A317EAR8_9PROT 
ID   A0A317EAR8_9PROT        Unreviewed;       882 AA.
AC   A0A317EAR8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:PWR22393.1};
GN   ORFNames=DKG75_10630 {ECO:0000313|EMBL:PWR22393.1};
OS   Zavarzinia compransoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Zavarziniaceae; Zavarzinia.
OX   NCBI_TaxID=1264899 {ECO:0000313|EMBL:PWR22393.1, ECO:0000313|Proteomes:UP000246077};
RN   [1] {ECO:0000313|Proteomes:UP000246077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1231 {ECO:0000313|Proteomes:UP000246077};
RA   Lee Y., Jeon C.O.;
RT   "Zavarzinia sp. HR-AS.";
RL   Submitted (MAY-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. 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|ARBA:ARBA00004496,
CC       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:PWR22393.1}.
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; QGLF01000002; PWR22393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317EAR8; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000246077; 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:UP000246077};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   882 AA;  96285 MW;  A74AD4CAA24CA445 CRC64;
     MDFEKYTERA RGFVQSAQGL ALRSNHQRFT PEHLAKVLLD DEQGLAASLI KAAGGRPEAA
     LAGIEAELAR LPKVEGQGAG QLYLAPETAR LFEQAEQVAK KAGDTFVTAE RLLLALVLAA
     GTPSAEILKK AGVTAQGLSK AIDDLRKGRT ADSASAEDSY DALKKYARDL TAAARDGKLD
     PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIAEG LALRIVNGDV PESLKHKQLM
     ALDLGALVAG AKYRGEFEER LKAILGEVTS SGDVILFIDE MHQLVGAGKT DGAMDASNLL
     KPALARGELH CVGATTLDEY RKHVEKDAAL ARRFQPVFVS EPTVEDTISI LRGLKEKYEL
     HHGVRISDVA LVAAATLSNR YITDRFLPDK AIDLVDESAS RLRMEVDSKP EALDELDRKI
     MQMQIEREAL KKEEDRASKE RLAKLEKDLA DLEQQSAEMT AKWRAEKDKL SVQQKLTEQL
     DAARSELEQA QRKGNLARAG EIAYGLIPDL TRKLEAAQAA TEAASMREAV TDEDIAAVVS
     RWTGIPVDKM LSGEREKLLK MEPLLASRVV GQPEAVAAVA NAVRRARAGL QDAARPIGSF
     LFLGPTGVGK TELTKALAEF LFDDDTAMVR VDMSEFMEKH AVSRLIGAPP GYVGYEEGGV
     LTEAVRRRPY QVILFDEVEK AHPDVFNVLL QVLDDGRLTD GQGRTVDFRN TVIILTSNLG
     GEFLAAEDAE VNPGRTRDQV MAVVRASFRP EFLNRLDEIV LFNRLGRGEM TGIVDIQLGR
     LRKLLADRKI VLDLDQAAKE WLAEAGYDPV YGARPLKRVI QRNLQNPLAE LILEGEVNDG
     DTVKVSAEAG QLVLNGKAVE ADNALVRKPS NPAFVSRVEG NA
//
DBGET integrated database retrieval system