GenomeNet

Database: UniProt
Entry: A0A1T5HAC8_9BACT
LinkDB: A0A1T5HAC8_9BACT
Original site: A0A1T5HAC8_9BACT 
ID   A0A1T5HAC8_9BACT        Unreviewed;       857 AA.
AC   A0A1T5HAC8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN03080601_02180 {ECO:0000313|EMBL:SKC17616.1};
OS   Alkalitalea saponilacus.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Alkalitalea.
OX   NCBI_TaxID=889453 {ECO:0000313|EMBL:SKC17616.1, ECO:0000313|Proteomes:UP000191055};
RN   [1] {ECO:0000313|EMBL:SKC17616.1, ECO:0000313|Proteomes:UP000191055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24412 {ECO:0000313|EMBL:SKC17616.1,
RC   ECO:0000313|Proteomes:UP000191055};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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   ---------------------------------------------------------------------------
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; FUYV01000012; SKC17616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5HAC8; -.
DR   STRING; 889453.SAMN03080601_02180; -.
DR   KEGG; asx:CDL62_17390; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000191055; 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:SKC17616.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SKC17616.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191055};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..142
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          401..435
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          465..526
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  95805 MW;  E0B85D014CB058C2 CRC64;
     MNLNQFTIKA QESVQQAVQI AAGLNHQAVE NGHLLKGIVQ TEEQLTKHLF GKLGISNVFQ
     ILDKIVESYP KVSGGEPYLG RAASDALQRA INKAKQMGDK FASIEHILIG IVGGADSVAK
     MLKDAGATEK GLEMAVHELR KGSKVDSQTA EDTYDALGRF AINLNDMARS GKLDPVIGRD
     DEIRRILQIL SRRTKNNPVL IGDPGVGKTA IAEGLAHRII NGDVPENLKS KQIFSLDMGA
     LVAGAKYKGE FEERLKAVVK EVLASDGEVV LFIDEIHTLV GAGKSEGAMD AANILKPALA
     RGELRAIGAT TLNEYQKYFE KDKALERRFQ IVMVDEPDTL SSISILRGLK ERYESHHKVR
     IRDEAIISAV ELSKRYISDR FLPDKAIDLI DEAASKLRLE MNSVPEEIDE IERKIKQLEI
     EREAIKREGD KAKMESLSFE ISELKQKHSS LMARWQEERS IIEKIQKFKA DIETYKFEAE
     KAEREGLYEK VAELRYGRIK DAEQSIEKLK ATLSEKQMDS AMIKEEVDSE DVAQVVSRWT
     GIPVNKMLKT ERQKLLAIEE ELHKRVVGQD EAISAVANAV RRSRAGLQDA RRPIGSFIFL
     GSTGVGKTEL AKALAGFLFD DENLMTRIDM SEYQERHSVS RLVGAPPGYV GYDEGGQLTE
     AVRRKPYSVV LLDEIEKAHP DVFNILLQVL DDGRLTDNKG RVVDFKNSIV IMTSNLGSHL
     LQESIDSGHS NIDDNVRAKM TELLRQTIRP EFLNRIDEII FFTPLDKEQV KEIVKMQFNG
     LVDVLKNQGV NIEITESAID WLVKAGFDPH YGARPVRRAI QHHVLNHLSK LILAESVQSD
     ESILVDADEN GLVFKNQ
//
DBGET integrated database retrieval system