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Database: UniProt
Entry: C5BQY8_TERTT
LinkDB: C5BQY8_TERTT
Original site: C5BQY8_TERTT 
ID   C5BQY8_TERTT            Unreviewed;       879 AA.
AC   C5BQY8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 96.
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:ACR10847.1};
GN   OrderedLocusNames=TERTU_1057 {ECO:0000313|EMBL:ACR10847.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR10847.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR10847.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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|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; CP001614; ACR10847.1; -; Genomic_DNA.
DR   RefSeq; WP_015816959.1; NC_012997.1.
DR   AlphaFoldDB; C5BQY8; -.
DR   STRING; 377629.TERTU_1057; -.
DR   KEGG; ttu:TERTU_1057; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_6; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000009080; Chromosome.
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:UP000009080};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          405..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   879 AA;  97755 MW;  9830178045236B6A CRC64;
     MRIDRLTNQL QIALSDAQSL AVGRDHNQIE PVHLLQAMLD QQGGTVRPLL ASAGFDVAGL
     RNELTKALEN LARIQNPTGD VHMSPELGRL LNLADKHAQK NGDKFISSES LLLAAMRDAN
     AELGKILNRY GTAARLQSAV DKVRGGEKVD NPDAEGNRQA LEKYTIDLTA RAEAGKLDPV
     IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVDGEVPE GLKNRRLLSL
     DLGALLAGAK FRGEFEERLK SVLNELGKQE GRVVLFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVVVDE PNEEDTIAIL RGLKERYELH
     HGVNISDSAI IAAAKLSQRY ITDRQLPDKA IDLIDEAGSR IRMEIDSKPE QMDRLERRLI
     QLKIEREAVK KDDDTAARKR LDLIESQIDE AERAYADLDE IWRAEKVSLQ GSQQIKSNLE
     QARLDLEAAR RAGDLGRMSE LQYGIIPELE KQLDMASQAE MHEMKLLRNK VTDEEIAEVV
     SKWTGIPVSK MLEGEREKLL RMEEVLHERV IGQSEAVIAV ANAVRRSRAG LSDPNRPNGS
     FLFLGPTGVG KTELCKALAE FLFDSQDAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSLVLLDEVE KAHPDVFNIL LQVLEDGRLT DGQGRTVDFR NTVVVMTSNL
     GSAAIQDIAQ NRAYDSINFD ESSSQDDSMQ NEHKYAAMKD AVMEVVAGHF RPEFINRIDE
     VVVFHPLGKP QIRGIADIQL GILRKRLHER ELKLDMSNEV MDKIAEAGFD PVYGARPLKR
     AIQQLIENPL AQEVLAGKFS PGQTIKVDLA GNDNVRFSV
//
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