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Database: UniProt
Entry: A0A151BU55_9MICO
LinkDB: A0A151BU55_9MICO
Original site: A0A151BU55_9MICO 
ID   A0A151BU55_9MICO        Unreviewed;       863 AA.
AC   A0A151BU55;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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=AZH51_17065 {ECO:0000313|EMBL:KYH43460.1};
OS   Branchiibius sp. NY16-3462-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Branchiibius.
OX   NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH43460.1, ECO:0000313|Proteomes:UP000075667};
RN   [1] {ECO:0000313|EMBL:KYH43460.1, ECO:0000313|Proteomes:UP000075667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH43460.1};
RA   Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT   "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT   sample.";
RL   Submitted (MAR-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|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:KYH43460.1}.
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DR   EMBL; LVCF01000042; KYH43460.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BU55; -.
DR   STRING; 1807500.AZH51_17065; -.
DR   Proteomes; UP000075667; 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:UP000075667};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..156
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          506..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          405..485
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   863 AA;  93244 MW;  982F41296BC5A982 CRC64;
     MDLQLTTKAQ EALSGAVQHA TAAGNPQVEP VHLLLALAEQ TDTTTGPLLE ATGTSASAVI
     SEAQRLIGQL PRSTGASVAQ PSMTRELLNV LERARQEMTA MGDTFTSTDH LLLALARTGG
     YGLNADALAA AIPQTRGGAK VTTQDPEAAF DALEKYGTDL TAVARDGKLD PVIGRDQEIR
     RVVQVLSRRT KNNPVLIGEP GVGKTAVVEG LAQRIVAGDV PESLRGKRLI SLDLGAMVAG
     AKYRGEFEER LKAVLEEIKN SGGQVITFID ELHTVVGAGA TGDSAMDAGN MLKPMLARGE
     LRLVGATTLD EYREHIEKDP ALERRFQQIY VGEPSVEDTI AILRGLKERY EAHHKVAIAD
     SALVAAASLS DRYITARQLP DKAIDLIDEA ASRLRMEIDS SPVEIDELRR AVDRLMMEQL
     HLENETDDAS KARLAKLQAD LADKEEQLAA LNARWEAEKA GLNKVGELKA QIDELRTQMD
     KLERDGDLGG ASKIRFGDLP ALEKQLEEAQ AAEASASTAG ASGEGPMVKD EVGADDIADV
     ISSWTGIPAG RLLEGETEKL LKMEEVLGER LIGQKAAVQA VSDAVRRSRA GVSDPDRPTG
     SFLFLGPTGV GKTELAKSLA DFLFDDERAM VRIDMSEYSE RHAVARLIGS PPGYVGYEEG
     GQLTEAVRRR PYSVVLLDEV EKAHPETFDI LLQVLDDGRL TDGQGRTVDF RNVILVMTSN
     LGSQFLIDPT VTREAQHEGV MATVRGTFKP EFLNRLDEIV IFDPLSKEEL ASIVDLQVAS
     FSKRLADRRI TLSVTDSARQ WLADEGYDPA YGARPLKRLV QKEVGDQLAK ELLAGEVLDG
     QTVVVDHPEG SDGLVLTPEP ALV
//
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