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Database: UniProt
Entry: A0A545T1U8_9GAMM
LinkDB: A0A545T1U8_9GAMM
Original site: A0A545T1U8_9GAMM 
ID   A0A545T1U8_9GAMM        Unreviewed;       878 AA.
AC   A0A545T1U8;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:TQV71207.1};
GN   ORFNames=FKG94_20195 {ECO:0000313|EMBL:TQV71207.1};
OS   Exilibacterium tricleocarpae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Exilibacterium.
OX   NCBI_TaxID=2591008 {ECO:0000313|EMBL:TQV71207.1, ECO:0000313|Proteomes:UP000319732};
RN   [1] {ECO:0000313|EMBL:TQV71207.1, ECO:0000313|Proteomes:UP000319732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R142 {ECO:0000313|EMBL:TQV71207.1,
RC   ECO:0000313|Proteomes:UP000319732};
RA   Wang G.;
RT   "Whole genome sequence for Cellvibrionaceae sp. R142.";
RL   Submitted (JUN-2019) 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:TQV71207.1}.
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DR   EMBL; VHSG01000022; TQV71207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A545T1U8; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000319732; 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:UP000319732};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          405..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   878 AA;  97571 MW;  0066D9A5E8DD185D CRC64;
     MRIDRLTNQL QIALSDAQSL AVGRDHNQLE PVHVLLAMLD QQGGTVRPLL AQAGFDVTGL
     RNELAKQLDN LARVQSPTGD VHMSAETGRL LNLADKRAQE VGDKFISSES LLLAAMHDGN
     SALGKLLNQF GDKQRLESAV DKVRGGETVD DPDAEGNRQA LEKYTIDLTA RAEAGKLDPV
     IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNKQLLSL
     DLGSLLAGAK FRGEFEERLK AVLNELSKQE GRIILFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC VGATTLDEYR KFIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
     HGVDITDSAI IAAAKLSQRY ITDRQLPDKA IDLVDEAASR IRMEIDSKPE EMDRLERRLI
     QLKIEREAVK KDTSESAKKQ LQLLDDDIEQ AERKFADLEE IWRAEKAALH GSHEIKSNLE
     QVRLDLEAAR RAGDLARMSE LQYGVIPELE KQLDMASQAE MMEMKLLRNK VTDEEIAEVV
     SKWTGIPVAK MLEGEREKLL RMEDALHRRV IGQQEAVVAV SNAVRRSRAG LADPNRPNGS
     FLFLGPTGVG KTELCKALAE FLFDSEDAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSVLLLDEVE KAHADVFNIL LQVLEDGRLT DGQGRTVDFR NTVVVMTSNL
     GSDRIQELAQ DRSFDTISFD SDENSDTAAN EHRRAAIKEA VMEVVASHFR PEFVNRIDEL
     VVFDPLGQAQ IRGIATIQLD LLRRRLAERE LKLELDDAVM DKLVQVGFDP VYGARPLKRA
     IQQQIENPLA QDVLAGKFAP GATVVGRLDE RGQLVFTG
//
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