ID   A0A1B1TVH9_9SYNE        Unreviewed;       997 AA.
AC   A0A1B1TVH9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   29-SEP-2021, entry version 28.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AWQ22_02235 {ECO:0000313|EMBL:ANV86385.1};
OS   Synechococcus sp. PCC 7117.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=195498 {ECO:0000313|EMBL:ANV86385.1, ECO:0000313|Proteomes:UP000092877};
RN   [1] {ECO:0000313|EMBL:ANV86385.1, ECO:0000313|Proteomes:UP000092877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7117 {ECO:0000313|EMBL:ANV86385.1,
RC   ECO:0000313|Proteomes:UP000092877};
RA   Liu Z., Li Z., Bryant D.A.;
RT   "Genome sequences of five ubiquitous Synechococcus strains found around the
RT   world.";
RL   Submitted (JUL-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:ARBA00011230}.
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; CP016477; ANV86385.1; -; Genomic_DNA.
DR   RefSeq; WP_065710048.1; NZ_CP016477.1.
DR   EnsemblBacteria; ANV86385; ANV86385; AWQ22_02235.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000092877; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016,
KW   ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          6..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          151..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          451..478
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          482..512
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COMPBIAS        151..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..949
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   997 AA;  111881 MW;  61FFDAA9809F3145 CRC64;
     MQPTDSSKFT EQAWDAIVKS QEIARRYRHQ NLEVEHLLLS LLEQEQEQGL AQTILTQTGV
     DGIRLQQQLE RFAQQQPKLM RGDQLYLGQG LDVMLDRAEA CRNSWQDDFI SVEHLLVGFA
     EDERIGRRSL KSFNLDPQDL ELKIKALKGS QKVTAQNQEE TGSTYGGSPL SKYGRDLTEQ
     AKDGKLDPVI GRDDEIRRVI QVLSRRSKNN PVLIGEPGVG KTAIAEGLAQ RIVNGDVPES
     LKNRQLMSLD MGSLIAGAKY RGEFEARLRS VLKEVTQSDG QIILFIDEVH TVVGAGSANG
     SMDAGNLLKP MLARGELRCI GATTLDEFRK HIEKDPALER RFQQVLVQQP TVEDTVSILR
     GLKERYELHH GVNITDSALV AAATLSNRYI TDRFLPDKAI DLVDEAAAKL KMEITSKPVE
     LEAIDRRLMQ LQMEQLSLKG EEQLGATSPA YLASKERLDR IDEEIKSLEI QQKDLSSQWL
     AEKNLIDEIN SLKEEEEQLR LQVEQAERAY DLNKAAQLKY GRLEGLQAEL SQKEVKLLEI
     QAAGDAMLRE QVTEADIAEI VARWTGIPVN RLMESERQKL LQLEGHLHER VIGQQEAVEA
     VSAAIRRARA GMKDPSRPIG SFMFMGPTGV GKTELARALA AFLFDSEEAM VRIDMSEYME
     KHAVSRLIGA PPGYVGYEEG GQLSEAVRRR PYSVVLLDEV EKAHKDVFNI LLQVLDDGRI
     TDSQGRVVDF RNTIIVMTSN IGSEFILSLS GDDANYDKMR DKVTGALRKN FRPEFLNRID
     ELIIFHTLKR DELREIVKLQ IHRIEKLLAD QKITLSLTDA ALDHVVEAGY DPTFGARPLK
     RAIQRELENP IANRILETDF MEGDRILVDC VEGALVFDRQ RPEREVPEVI SEEAIAPAPE
     EQPIETEEAS ITEAEILPVV APDEIVVAEA ELDEPDDDWG EDETTVSFDA EQPDDQWFGA
     DEPEQTANGL ESPIRETNPP AYVGADSDSE ENWLDSI
//