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Database: UniProt
Entry: A0A2A8CTQ9_9BACT
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ID   A0A2A8CTQ9_9BACT        Unreviewed;       893 AA.
AC   A0A2A8CTQ9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:PEN11079.1};
GN   ORFNames=CRI94_16795 {ECO:0000313|EMBL:PEN11079.1};
OS   Longibacter salinarum.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC   Longibacter.
OX   NCBI_TaxID=1850348 {ECO:0000313|EMBL:PEN11079.1, ECO:0000313|Proteomes:UP000220102};
RN   [1] {ECO:0000313|EMBL:PEN11079.1, ECO:0000313|Proteomes:UP000220102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 52045 {ECO:0000313|EMBL:PEN11079.1,
RC   ECO:0000313|Proteomes:UP000220102};
RA   Goh K.M., Shamsir M.S., Lim S.W.;
RT   "Draft genome of Longibacter Salinarum.";
RL   Submitted (OCT-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|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:PEN11079.1}.
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DR   EMBL; PDEQ01000012; PEN11079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8CTQ9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000220102; 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:UP000220102};
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          405..530
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   893 AA;  99505 MW;  BC1FB86E81CEE1E4 CRC64;
     MNLQKFTVKA QEAVQSAMEI AASNNHQGVE PAHVLKAFLS DTEGITTSIL RRLGASVDTL
     RQRTDSALDK LPKVTGASVS GQYLGDELKK VFDRARAEAD LMNDEYVSTE HLLIGLVESK
     GEVGQALRDQ GASKDKVRDV LEDVRGGQSA DDPHAESRYE ALDRFARDLN DLARRGKIDP
     VIGRDQEIRR VLQILSRRTK NNPVLVGEAG VGKTAIAEGI ATRIVQGDVP ESMKSKRIVA
     LDMGALVAGA KYRGEFEDRL KAVVKEVSES DGELILFIDE LHTLIGAGAA EGAMDAANIL
     KPALARGELR AIGATTLDEY KYIEDDRALE RRFQKVVVDE PSVDDTISIL RGLKERYEVH
     HGVRIQDSAI ISAADLSNRY ITDRQLPDKA IDLIDEAAAR LRIEIDSMPA DLDQLDREIR
     QLEIEREAIK RDEDEEKLEN INHQIASLED ERDALKTRWK EEKDLIQTAR QAKEKIDELR
     VEAENLEREG KYDRVAEIRY GEIPDLEKQA EEANEKLQEV QQDGALLKEE VDGEDIAEIV
     SNWTGIPVSK MLESERQKLV RMEEELSKRV IGQPEAIEVV SDAVRRGRTG LQEENRPIGS
     FLFLGTTGVG KTELAKTLAA FLFNDEDAMV RIDMSEYQEK HTASRLIGAA PGYVGYEEGG
     QLTEAVRRKP YSVVLLDEIE KAHPEIFNVL LQVLDDGRLT DNQGRTVDFT NTIIIMTSNM
     GSEVITEKMD SVDGGYLSDL ERQELEEKLL KMLRQRLRPE FLNRIDEVVT FRSLGRSHIR
     EIVELQFNRI AGIAKKSHNL QLQLSDAAKD WLADRGFDPA FGARPLKRVM QRQVSNQLSK
     ELLGGSVEDG DTVRIDLAPE QNHLTFEAVR TGADGTGEAA ETAEPAGDGA VSM
//
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