ID A0A501XEE8_9SPHN Unreviewed; 866 AA.
AC A0A501XEE8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:TPE58674.1};
GN ORFNames=FJQ54_16640 {ECO:0000313|EMBL:TPE58674.1};
OS Sandaracinobacter neustonicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Sandaracinobacter.
OX NCBI_TaxID=1715348 {ECO:0000313|EMBL:TPE58674.1, ECO:0000313|Proteomes:UP000319897};
RN [1] {ECO:0000313|EMBL:TPE58674.1, ECO:0000313|Proteomes:UP000319897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28131 {ECO:0000313|EMBL:TPE58674.1,
RC ECO:0000313|Proteomes:UP000319897};
RA Lee I., Jang G.I., Hwang C.Y.;
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC 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:TPE58674.1}.
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DR EMBL; VFSU01000034; TPE58674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A501XEE8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000319897; 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:UP000319897};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 94380 MW; 0F4543BAEF2E5762 CRC64;
MNIEKFTDRA KGFLQAAQTI ALREQHQRVT TGHLLKALLD DDQGMATGLI QAAGGDAKRA
RVAVDTAVSK LPKVSGSGAQ MQWDQDVARL LDQAEQIASK AGDSFVTVER LLLALALAPD
TEAGKALKEA GVTAQGLNAA IEQLRKGRAA HSASAEESYD ALKKYGRDLT QVARDGKLDP
VIGRDEEIRR TIQVLARRSK NNPVLIGEPG VGKTAIAEGL ALRIAKGDVP DGLKDKTLFA
LDMGALIAGA KYRGEFEERL KAVIDEVKAA EGQVILFIDE MHTLVGAGKS EGSMDASNLL
KPALSRGEVH VIGATTLDEY RKHVEKDAAL ERRFQPVFVG EPTVEDTISI LRGLKEKYEL
HHGVRITDSA LVSAATLSNR YISDRFLPDK AIDLMDEAAS RLRMEVESKP EEIEALDRRI
IQLKIEREAL TKEKDDASRG RLATLEAELA DLELEAGNLT ARWEGEKEKL SNATKIKEAL
DQARFEVEQA QRQGNFARAG ELTYGVIPDL EAKLADAEKA SESAMVREEV TSEDIAAVVS
RWTGIPVTRM MEGEREKLLN MEAELGKRVI GQDDAVKAVS KAVRRARAGL QDPNRPLGSF
LFLGPTGVGK TELTKALADF LFDSSDAMVR IDMSEFMEKH SVARLIGAPP GYVGYDEGGV
LTEAVRRRPY QVVLFDEVEK AHSDVFNILL QVLDDGRLTD GQGRTVDFSN TLIILTSNLG
SQFIAALPDG ADVKQAEAQV MDVVRGHFRP EFLNRLDEII LFHRLALQHM GAIVDIQLNH
VRKLLKDRKI SLVLSEGAQS WLARVGYDPV YGARPLKRAI QKHLVDPLAE LLLAGDVPDG
ATVTVTDGDG QLQLAVSTEA GVQAAA
//