ID A0A081KEB1_9GAMM Unreviewed; 860 AA.
AC A0A081KEB1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=GV64_18690 {ECO:0000313|EMBL:KEI72487.1};
OS Endozoicomonas elysicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI72487.1, ECO:0000313|Proteomes:UP000027997};
RN [1] {ECO:0000313|EMBL:KEI72487.1, ECO:0000313|Proteomes:UP000027997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI72487.1,
RC ECO:0000313|Proteomes:UP000027997};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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:KEI72487.1}.
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DR EMBL; JOJP01000001; KEI72487.1; -; Genomic_DNA.
DR RefSeq; WP_020584837.1; NZ_JOJP01000001.1.
DR AlphaFoldDB; A0A081KEB1; -.
DR STRING; 305900.GV64_18690; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000027997; 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 78, MITOCHONDRIAL; 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:UP000027997};
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 860 AA; 95706 MW; 4E8BCBB8206BC647 CRC64;
MRMDRLTSKL QSALADAQSL AIGKDNSQID PVHLLLALID QKGGSVKPLL MQVGFDVDAL
RSELNNMLEQ LPQVTSPTGD IQTSQALYRM LNLTDKKAQQ AGDQFISSET MLLVMMEDSG
PLGKLLSSQG VSQKALENAI KNIRGGASIN DPNAEDNRNS LSKYTIDLTE RAEEGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVIIGEPGV GKTAIVEGLA QRIVNGEVPE GLKGKRVLSL
DMGALIAGAK FRGEFEERLK AVLNDLAKQE GQIILFIDEI HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVMVDE PTEEDAIAIL RGLKERYEAH
HGVDITDPAI IAAVKLSQRY ITDRQLPDKA IDLIDESASR IRMEMDSKPE AMDRLERRLI
QLKIEQEALK KEDDDASKER LTKLKEQVGE LEREYSDMED VWKAEKAQLQ GGQKLREEKE
KLLIELEAAR RAGDLTKMSE IQYGTLPELD KQLAQADVLD TGEHQLLRNR VTEEEIAEVV
SKWTGIPVAK MLEGEKEKLL RMEDSLHKRV VGQDEAVVAV SNAVRRSRAG LADPNRPNGS
FMFLGPTGVG KTELCKALAE FLFDTEDAII RIDMSEFMEK HSVSRLLGAP PGYVGYEEGG
YLTEAVRRKP YSLVLLDEVE KAHPDVFNIL LQVLEDGRLT DGQGRTVDFK NTVIVMTSNL
GSDLIQTFQN KETGETNFEE LKNTLIEVVG NHFRPEFVNR IDEVVVFHPL GESQIKSIAR
IQLANLDRRL ADNNLKLELS EEAMDQLAEV GFDPVYGARP LKRAIQRSIE NPLAEAILSG
RFKPGDTINI VLKDGQLDFA
//
