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Database: UniProt
Entry: A0A1Y4U073_9FIRM
LinkDB: A0A1Y4U073_9FIRM
Original site: A0A1Y4U073_9FIRM 
ID   A0A1Y4U073_9FIRM        Unreviewed;       866 AA.
AC   A0A1Y4U073;
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=B5E62_06455 {ECO:0000313|EMBL:OUQ51200.1};
OS   Lachnoclostridium sp. An118.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965547 {ECO:0000313|EMBL:OUQ51200.1, ECO:0000313|Proteomes:UP000199786};
RN   [1] {ECO:0000313|Proteomes:UP000199786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An118 {ECO:0000313|Proteomes:UP000199786};
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:OUQ51200.1}.
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DR   EMBL; NFLQ01000005; OUQ51200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4U073; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199786; 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:UP000199786};
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          404..491
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  97155 MW;  0F2BF36E995D40DC CRC64;
     MNINKFTQKS LQAVQDCEKT AMEYGNQEIE QEHLLYALLT QDDSLILKMM EKMGLDKNLV
     VDRVEQAIAK RPKVQGGQPY VGQYLNKALI SAEDEMKQMG DEYVSVEHLF LALLKHPSRE
     IKQLFRELGI SREGFLQALS TVRGNQKVTS DNPEATYDTL NKYGTDLVDR ARDQKLDPVI
     GRDSEIRNVV RILSRKTKNN PVLIGEPGVG KTAVVEGLAQ RIVSGDVPEA LKDKTIFSLD
     MGALVAGAKY RGEFEERLKA VLEEVKNSDG KIILFIDELH TIVGAGKTDG AMDAGNMLKP
     MLARGELHCI GATTLDEYRQ YIEKDAALER RFQPVMVDEP TVEDAISILR GLKERYEVFH
     GVKITDGALV AAATLSHRYI SDRFLPDKAI DLVDEACAMI KTELDSMPAE LDEMRRKVMQ
     LEIEEAALKK EDDRLSQDRL AHLQQELAEL RAEFATRKAQ WDNEKVSVER VQKLREQIEQ
     IRGDIQKAQQ SYDLEKAAEL QYGKLPELQK MLEAEEAKVK DEDLSLVHES VTEDEIAKIV
     SKWTGIPVAK LNESERSKTL HLADELHKRV VGQDEAVELV TEAIIRSKAG IKDPTRPIGS
     FLFLGPTGVG KTELAKALAQ SLFDDENNMV RIDMSEYMEK YSVSRLIGAP PGYVGYDEGG
     QLTEAVRRKP YSVVLFDEVE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNI
     GSAYLLEGID ENGNISEASQ KAVTDDLRAH FRPEFLNRLD EIIMFKPLTK DNIYHIIDLL
     VADVNRRLRE KEVGIELTEA AKARIVEGGY EPMYGARPLK RYLQKNVETT AARLMLEGNV
     GSGDTILIDD QDGKLTARVK EGLTAV
//
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