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
//