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Database: UniProt
Entry: A0A1Y4IIP4_9FIRM
LinkDB: A0A1Y4IIP4_9FIRM
Original site: A0A1Y4IIP4_9FIRM 
ID   A0A1Y4IIP4_9FIRM        Unreviewed;       859 AA.
AC   A0A1Y4IIP4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-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=B5F29_05875 {ECO:0000313|EMBL:OUP20194.1};
OS   Lachnoclostridium sp. An196.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965583 {ECO:0000313|EMBL:OUP20194.1, ECO:0000313|Proteomes:UP000199780};
RN   [1] {ECO:0000313|Proteomes:UP000199780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An196 {ECO:0000313|Proteomes:UP000199780};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-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   -!- 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:OUP20194.1}.
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DR   EMBL; NFJZ01000004; OUP20194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4IIP4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199780; 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:UP000199780};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          411..525
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   859 AA;  97052 MW;  0224D076DB28E2A0 CRC64;
     MNFQKFTQKS IQAVNDLEKV ALEYGNQEIE QEHLLYSLLT QEESLIARLI SKMDIDSTLF
     KERVEEALNK RVKVSGGQPY IGQYLNKALV SAEDEAKRMG DEYVSVEHLF LSLLDNPSPT
     IKTLFRENGI TREKFLQALS TVRGNQRVTT DNPEATYDTL NKYGYDLVEK AREQKLDPVI
     GRDSEIRNVV RILSRKTKNN PVLIGEPGVG KTAVVEGLAE RIVRGDVPEG LKDKKIFALD
     MGALVAGAKY RGEFEERLKA VLEEVRKSEG QIILFIDELH LIVGAGKTDG AMDAGNMLKP
     MLARGELHCI GATTLDEYRQ YIEKDAALER RFQQVLVDEP TVEDTISILR GLKERYEVYH
     GVKITDSALV AAASLSHRYI SDRFLPDKAI DLVDEACALI KTEMDSMPTE LDELRRKVLQ
     LEIEEAALKK ETDRLSRDRL AALQKELADL RDEFNNKKAQ WDDEKHSVEK LSKLREDIEN
     VNKEIQNAQR NYDLEKAAQL QYGKLPQLQK QLEEEEEKVK KQDLSLVHES VTDEEIARIV
     SRWTGIPVAK LTESERNKTL HLDGELHKRV IGQDEAVQKV ADAIIRSKAG IKDPTKPIGS
     FLFLGPTGVG KTELAKTLAA SLFDDEQNMV RIDMSEYMEK YSVSRLIGAP PGYVGYEEGG
     QLTEAVRRHP YSVVLFDEVE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNI
     GSSYLLDGID EKGDIRPESE EMVMKDLRSH FRPEFLNRLD EIILFKPLTK DNIGHIVDLL
     IADLNRRLAD KELHLQLTDS AKAFVVENGY DPVYGARPLK RYLQKYVETM AARYILSGNV
     QAGSTMTVDC DGQNLTIAS
//
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