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Database: UniProt
Entry: A0A2S5KQU4_9PROT
LinkDB: A0A2S5KQU4_9PROT
Original site: A0A2S5KQU4_9PROT 
ID   A0A2S5KQU4_9PROT        Unreviewed;       858 AA.
AC   A0A2S5KQU4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=C4K68_14160 {ECO:0000313|EMBL:PPC76636.1};
OS   Proteobacteria bacterium 228.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=2083153 {ECO:0000313|EMBL:PPC76636.1, ECO:0000313|Proteomes:UP000238196};
RN   [1] {ECO:0000313|EMBL:PPC76636.1, ECO:0000313|Proteomes:UP000238196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=228 {ECO:0000313|EMBL:PPC76636.1,
RC   ECO:0000313|Proteomes:UP000238196};
RA   Krishnan R., Ramesh Kumar N.;
RT   "novel marine gammaproteobacteria from coastal saline agro ecosystem.";
RL   Submitted (FEB-2018) 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:PPC76636.1}.
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DR   EMBL; PRLP01000045; PPC76636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5KQU4; -.
DR   OrthoDB; 5287200at2; -.
DR   Proteomes; UP000238196; 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:UP000238196};
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          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   858 AA;  95644 MW;  4871BDAA222A5741 CRC64;
     MRIDRFTTKL QEALNDAVSL AVGRDHNQLE PLHLFASLLE QQGGSTRSIL SQAGFDVAKL
     RRELDKELGK LATVKQHDGD VRPSERFARL LNLADKASQQ NGDQYISSEL VVLAAMDDKS
     GLGDVLRAQG IRKEQLEAVI NKVRGGENVS DPNAEEKRDA LKKYTIDLTA RAVAGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKDKQVLSL
     DMGALIAGAK FRGEFEERLK AVLNELAKEE GRVILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSVEDTIAIL RGLKERYEVH
     HGVDITDSAI IAAAKLSQRY ITDRQLPDKA IDLIDEAGSR IRMEMDSKPE EMDRLDRRLI
     QLKMEREALK KETDKASKAR LDDLEQVIGK LEREYADLEE VWKTEKAALQ GSQKIKEQLE
     QARVDMEQAR RSGNLARMSE LQYGVIPDLE KQLDMASQAE MMDMQLLRNR VSEEEVAEVV
     SKWTGIPISK MLEGEREKLL RMEDALHESV IGQDEAVVAV ANAVRRSRAG LADPNRPNGS
     FLFLGPTGVG KTELCKALAR FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTETVRRKP YSVVLLDEVE KAHPDVFNIL LQVLEDGRLT DGQGRTVDFR NTVIVMTSNL
     GSDIIQAYTS SDTLYEEMKD KVMDVVATHF RPELVNRIDE VVVFHSLGQS QVRGIADIQI
     GRLGQRLQER DLQLEITPEA LDHLVAVGFD PVYGARPLKR SIQRHLENPL ANEILSGHFA
     PGSTIKVSLV DGQLVFGQ
//
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