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Database: UniProt
Entry: A0A218QJ99_9CYAN
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ID   A0A218QJ99_9CYAN        Unreviewed;       872 AA.
AC   A0A218QJ99;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=NIES4075_29020 {ECO:0000313|EMBL:GAX41905.1};
OS   Tolypothrix sp. NIES-4075.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX41905.1, ECO:0000313|Proteomes:UP000198313};
RN   [1] {ECO:0000313|EMBL:GAX41905.1, ECO:0000313|Proteomes:UP000198313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX41905.1,
RC   ECO:0000313|Proteomes:UP000198313};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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}.
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:GAX41905.1}.
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DR   EMBL; BDUC01000003; GAX41905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218QJ99; -.
DR   OrthoDB; 438311at2; -.
DR   Proteomes; UP000198313; 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:UP000198313};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          6..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..535
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   872 AA;  98672 MW;  323209E1AF2C3DE7 CRC64;
     MQPTNPNQFT EKAWEAIAHT PDIAKQYQLQ QIESEHLMKA LLEQEGLASA VFTKAGVNLQ
     KLRDRTEQFI QRQPKVSGSS SSVYLGRSLD TLLDRADGYR KEFQDEYISI EHLLLAYAKD
     DRFGKSLFQE FGLDEGKLKN IIKQIRGNQK VTDQNPEGKY EALEKYGRDL TEAARQGKLD
     PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIVAGDV PQSLKDRRLI
     ALDMGALIAG AKFRGEFEER LKAVLKEVTE SGGNIVLFID EIHTVVGAGA TQGAMDAGNL
     LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQQVYV DQPSVEDTIS ILRGLRERYE
     NHHGVKISDS ALVAAAILSS RYISDRFLPD KAIDLVDEAA ARLKMEITSK PEELDEIDRK
     ILQLEMERLS LQKESDAGSR ERLERLEKEL ADFKEEQRTF NTQWQSEKDI ITKIQSVKQD
     IERVNLEIQQ AERDYDLNRA AELKYGKLTD LHRQLEAAES ELAQTQHSGK SLLREEVTEG
     DIAEVISKWT GIPISKLVES EKEKLLQLED ELHHRVVGQD EAVTAVADAI QRSRAGLADP
     NRPIASFIFL GPTGVGKTEL AKALAAYLFD TEEALVRIDM SEYMEKHAVS RLIGAPPGYV
     GYDEGGQLTE AIRRRPYAVL LFDEIEKAHP DVFNIFLQIL DDGRVTDAQG HTVDFKNTII
     IMTSNIGSQY ILDVSGDDSR YDEMRHRVME AMRNSFRPEF LNRIDETIIF HALHKQELRH
     IVQLQVNRLR QRLGDRKISL KLSDSALDFL AEVGYDPVFG ARPLKRAIQR ELETQIAKAI
     LRGEFNNGDT IFVDVQNERL SFNRLPAEVF TG
//
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