GenomeNet

Database: UniProt
Entry: A0A1I7IK36_9CLOT
LinkDB: A0A1I7IK36_9CLOT
Original site: A0A1I7IK36_9CLOT 
ID   A0A1I7IK36_9CLOT        Unreviewed;       865 AA.
AC   A0A1I7IK36;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN04487886_11232 {ECO:0000313|EMBL:SFU73248.1};
OS   Clostridium sp. DSM 8431.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1761781 {ECO:0000313|EMBL:SFU73248.1, ECO:0000313|Proteomes:UP000198524};
RN   [1] {ECO:0000313|EMBL:SFU73248.1, ECO:0000313|Proteomes:UP000198524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8431 {ECO:0000313|EMBL:SFU73248.1,
RC   ECO:0000313|Proteomes:UP000198524};
RA   de Groot N.N.;
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. {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; FPBY01000123; SFU73248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7IK36; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198524; 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:SFU73248.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFU73248.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198524};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          417..497
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   865 AA;  97661 MW;  51E63D9E89F53EA4 CRC64;
     MDIDKMTLRV QKALSDANVI AVRNDHQQIE TIHVFAALME QEDGLIPNIL NKMGISTKEV
     TAKINSKLSS MPKVLGEGAN SSGVYITRQV ESVLVKAEEI SKQFKDSFVS VEHLMLALMD
     VDSNGPVGEI LKSFNINKKD FMQVLEQVRG NQKVDTQDPE GTYDALAKYG TNLVELAKKH
     KLDPVIGRDE EIRRAIRILS RRTKNNPVLI GEPGVGKTAI VEGLAERIVR GDVPEGLKDR
     IIFSLDMGSL IAGAKYRGEF EERLKAVLKE VQSSEGKIIL FIDEIHTIVG AGKTDGAMDA
     GNLIKPLLAR GELHCIGATT FDEYRQYIEK DKALERRFQP VIVNEPTVED TISILRGLKE
     KFEIHHGIRI HDSAIVAAAK LSDRYVQDRY LPDKAIDLID EAGSMVRSEI DSLPTELDVL
     RRKKFQLETE KEALEKENDE GSKKRLAALN KELADIKEKD DEMTAKYEKE KEHIMALRDL
     KTQLDDARGE VEKYQRQYDY NKVAELQYST IPRLEEAIAK KEAEVKENYD GALLKEEVTE
     EEISEVLSKW TGIPVNNLLE GEREKLLRLD EELQRRVIGQ DRAVEAVSSA ILRARAGLKD
     ENKPIGSFLF LGPTGVGKTE LAKTLARTLF DTEDAMIRID MSEYMEKHAV SRLVGAPPGY
     VGYEQGGQLT EAVRRRPYSV LLFDEIEKAH PDVFNMFLQI LDDGRLTDNK GKTVDFKNTI
     IIMTSNIGSQ YLLDNEGEEV SDENRELVMQ ALRSKFKPEF LNRVDDTIMF KPLSEDGIKK
     IIEIFLDEVR ERLKDRNITL EITDKAKSIL AREGYDPVYG ARPLKRYIQN TLENSLARKI
     IKGEVHYGST VVVDATEDEL TLSTR
//
DBGET integrated database retrieval system