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Database: UniProt
Entry: A0A4R5TWD5_9MICC
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ID   A0A4R5TWD5_9MICC        Unreviewed;       870 AA.
AC   A0A4R5TWD5;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:TDK25422.1};
GN   ORFNames=E2F48_09155 {ECO:0000313|EMBL:TDK25422.1};
OS   Arthrobacter crusticola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=2547960 {ECO:0000313|EMBL:TDK25422.1, ECO:0000313|Proteomes:UP000295411};
RN   [1] {ECO:0000313|EMBL:TDK25422.1, ECO:0000313|Proteomes:UP000295411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLN-3 {ECO:0000313|EMBL:TDK25422.1,
RC   ECO:0000313|Proteomes:UP000295411};
RA   Lixiong L.;
RT   "Arthrobacter sp. nov., an bacterium isolated from biocrust in Mu Us
RT   Desert.";
RL   Submitted (MAR-2019) 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|ARBA:ARBA00004496,
CC       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:TDK25422.1}.
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DR   EMBL; SMTK01000003; TDK25422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R5TWD5; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000295411; 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 78, MITOCHONDRIAL; 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:UP000295411};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   870 AA;  93994 MW;  02034EE39D1D9D80 CRC64;
     MDAKFTTKSQ EALSAAAMNA STAGNPQVET PHFLKALMDQ REGIAVALLK AAGASPDDIS
     VQASTAIRAL PSSSGSNVAQ AQFSRGALQV ISAAQQEAEA LGDQFVSTEH LLLGLAADAG
     PAGRILREAG ISRDALAAAL PGVRGDRRVT SADPENTFQA LEKFGVDLTE LARAGRLDPV
     IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRMVAGDVPE SLRGKSLISL
     DLGSMIAGAK YRGEFEERLK AVLEEIRSSN GQVVTFIDEL HTVVGAGASE GSMDAGNMLK
     PMLARGELRL IGATTLDEYR ENVEKDPALE RRFQQVYVGE PSVEDTIGIL RGLKERYEAH
     HKVSIADSAL VAAATLSNRY ISGRQLPDKA IDLVDEAASR LRMEIDSAPV EIDELRRAID
     RMRMEELALE RETDEASQER LEDLRAVMAD RQEQLSALNA RWEAEKAGLN RVGDLKASLD
     ELRSQADKAQ REGDLETASR ILYGEIPQVQ RELDAAQAAE QESAGETLEL MVAEEVTAND
     IAEVISAWTG IPAGRMLQGE SQKLLHMEEV IGSRLIGQSK AVASVSDAVR RARAGVSDPN
     RPTGSFLFLG PTGVGKTELA KALADFLFDD ERSMVRIDMS EYSEKHSVAR LVGAPPGYVG
     YEEGGQLTEA VRRRPYSVVL LDEVEKAHPE VFDILLQVLD DGRLTDGQGR TVDFRNVILV
     LTSNLGSQFL MDPSLDDAAR RQAVMATVNA SFRPEFLNRL DDVIIFDALS LDELSKIVDL
     QVEALGKRLQ ERRLTLEVTP AASEWLALTG FDPAYGARPL RRLVQREIGD QLARGILAGE
     IADGDRVLVD RDGGAGVDGQ GEGLSLRAVA
//
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