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}.
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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
//