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
//