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Database: UniProt
Entry: A0A501XEE8_9SPHN
LinkDB: A0A501XEE8_9SPHN
Original site: A0A501XEE8_9SPHN 
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
//
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