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Database: UniProt
Entry: A0A0U3AYE3_9ALTE
LinkDB: A0A0U3AYE3_9ALTE
Original site: A0A0U3AYE3_9ALTE 
ID   A0A0U3AYE3_9ALTE        Unreviewed;       856 AA.
AC   A0A0U3AYE3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AT746_13380 {ECO:0000313|EMBL:ALS99151.1};
OS   Lacimicrobium alkaliphilum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Lacimicrobium.
OX   NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS99151.1, ECO:0000313|Proteomes:UP000068447};
RN   [1] {ECO:0000313|EMBL:ALS99151.1, ECO:0000313|Proteomes:UP000068447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YelD216 {ECO:0000313|EMBL:ALS99151.1,
RC   ECO:0000313|Proteomes:UP000068447};
RA   Kim S.-G., Lee Y.-J.;
RT   "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; CP013650; ALS99151.1; -; Genomic_DNA.
DR   RefSeq; WP_062481104.1; NZ_CP013650.1.
DR   AlphaFoldDB; A0A0U3AYE3; -.
DR   STRING; 1526571.AT746_13380; -.
DR   KEGG; lal:AT746_13380; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000068447; Chromosome.
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:UP000068447};
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   856 AA;  95613 MW;  1781DF53E03E87CF CRC64;
     MRLDKMTSKF QLAISDAQSL ALGRDHQYIE PAHLMMALLN QEGGSVKPLM EQTGVNSNSL
     RSALSELIER LPQVQGVGGD VQLGKDTAVL LNLCDKIAQK RKDDYITSEI FVLAAMQDKG
     KLGETLRQLG LTEQKVEKAI EKLRGGQKVT DPNAEDVRQA LEKFTTDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKDKKVLSL
     DMGALVAGAK YRGEFEERLK AVLNELSKEE GRVILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALSRGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDQ PNVEDTIAIL RGLKERYELH
     HAVNITDPAI VAAAALSHRY ISDRQLPDKA IDLIDEAASS IRLQIDSKPE EMDRLERRII
     QLKLEEQALS KETDDASHKR LELIEQEREQ LEQKFKQLEK IWNTEKSAMQ GTQHIKSELE
     QAKLDLEIAR RASDLSRMSE LQYGRIPELE RRLELADEAQ GQETTLLKNK VTETEIADVL
     SRWTGIPVAK MLEGERDKLL RMEDALHDRV IGQSEAVTSV ANAIRRSRAG LADPNRPIGS
     FLFLGPTGVG KTELCKALAE FLFDSADSMV RIDMSEFMEK HSVSRLVGAP PGYVGYDEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVVIMTSNL
     GSDVIQDKHK ESQYEEMKAL VMNVVVQQFR PEFINRIDDT VVFHPLGHEQ IREIAEIQLA
     SLKARLAEKG YQLELTQKAL DKLADAGFDP VYGARPLKRA IQHQLENPLA QKLLSGNLPP
     DSVIKVDADE NGLVFS
//
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