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Database: UniProt
Entry: A0A161KJU2_9SYNE
LinkDB: A0A161KJU2_9SYNE
Original site: A0A161KJU2_9SYNE 
ID   A0A161KJU2_9SYNE        Unreviewed;       874 AA.
AC   A0A161KJU2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=FLM9_1005 {ECO:0000313|EMBL:CZB19333.1};
OS   Candidatus Synechococcus spongiarum.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=431041 {ECO:0000313|EMBL:CZB19333.1, ECO:0000313|Proteomes:UP000182631};
RN   [1] {ECO:0000313|Proteomes:UP000182631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   liu f.;
RL   Submitted (FEB-2016) 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|ARBA:ARBA00004496,
CC       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; FITM01000107; CZB19333.1; -; Genomic_DNA.
DR   RefSeq; WP_074457483.1; NZ_FITM01000107.1.
DR   AlphaFoldDB; A0A161KJU2; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000182631; 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:UP000182631};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          5..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          853..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          413..527
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   874 AA;  97113 MW;  A02983DAE1CAD84C CRC64;
     MQPTPETFTL KAWEAVSSAH TLAKARKSQT LESEHLLKAL LEQKDLAVRI LEAAAVDVAA
     LDSNLEQFLA RQPKLGAPPD TVSLGSSLDQ LLDRAEKEQQ AWKDQFIATE HLVLALCEDS
     RCGKTLLQAL GGRRQAIKDA VQSIRGNQRV TSQSPEATYE ALQNYGCDLT EAARQGKLDP
     VIGRDEEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEAL AQRIVNGDVP TALQNRRLVS
     LDMGALIAGA KYRGEFEERL KAVLKEVTSG KDQIVLFIDE VHTVVGAGAA GGSMDASNLL
     KPMLARGELR CIGATTLDEH RRYIEKDAAL ERRFQQVVVP QPTVEDTISI LRGLKERYEV
     HHGVRIADNA LVAAAVLSSR YINDRFLPDK AIDLVDEAAA HLKTEITSKP EEIDEIDRKI
     LQLEMEKLSL AKESDAASRE RLTRINQDLA NLTEQQRALM AQWTQEKGAL DDLQGLKEQI
     EQVQVKLEQA KRNYDLNKAA ELEYGTLAEL QQRLQKGEQQ LQDNEKRLLR QTISEEDVAE
     VVSKWTGIPV QRLAQSELQK LLDLEQRLQA RVVGQQEAVG SVADAIQRSR AGLADPRRPI
     ASFLFLGPTG VGKTELCKAL AEQLFDDEAA IVRLDMSEYM ERHAVSRLIG APPGYVGHEE
     GGQLTEAVRR KPYAVILLDE VEKAHPEVFN VLLQVLDDGR ITDSQGRTVN FTNSIVILTS
     NIASQAILDL AGDDSRHGEM EARVKQALGT HFRPEFLNRI DEIIIFHALR KQELRRIVEL
     QVTQLQQRLQ EKGLSLVLIP EACDWLAAVG YDPVYGARPL RRAIQKHLET PMAKAILRGD
     FRKGDTIVVE PEEGRGSQLR MGKGAHPEMV TAAR
//
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