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Database: UniProt
Entry: A0A0U4B5T5_9ACTN
LinkDB: A0A0U4B5T5_9ACTN
Original site: A0A0U4B5T5_9ACTN 
ID   A0A0U4B5T5_9ACTN        Unreviewed;       871 AA.
AC   A0A0U4B5T5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AERYTH_01230 {ECO:0000313|EMBL:ALX03417.1};
OS   Aeromicrobium erythreum.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=2041 {ECO:0000313|EMBL:ALX03417.1, ECO:0000313|Proteomes:UP000067689};
RN   [1] {ECO:0000313|EMBL:ALX03417.1, ECO:0000313|Proteomes:UP000067689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR18 {ECO:0000313|EMBL:ALX03417.1,
RC   ECO:0000313|Proteomes:UP000067689};
RX   PubMed=1883712;
RA   Miller E.S., Woese C.R., Brenner S.;
RT   "Description of the erythromycin-producing bacterium Arthrobacter sp.
RT   strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.";
RL   Int. J. Syst. Bacteriol. 41:363-368(1991).
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; CP011502; ALX03417.1; -; Genomic_DNA.
DR   RefSeq; WP_067853579.1; NZ_CP011502.1.
DR   AlphaFoldDB; A0A0U4B5T5; -.
DR   STRING; 2041.AERYTH_01230; -.
DR   KEGG; aer:AERYTH_01230; -.
DR   PATRIC; fig|2041.4.peg.254; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000067689; 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:UP000067689};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          851..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          414..494
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  94074 MW;  E259F95C654550CD CRC64;
     MDLSNLTTRS QQALAAAMQQ AAAAGNPAIE PAHVLTALLA QDGGTAVPLL QATGVDAGAV
     RTELQGVIGA LPSAAGSSVQ NPGLSRSTHE VLQRAADLAG ELGDEFISTE HLVVGVATVD
     SPAKDVLTSR GATPDALRAA FETVRGGARV TSADAEDTYQ ALEKYGVDLT AVAREGKLDP
     VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVDGDVP ESLRGRRLIS
     LDLGAMVAGA KYRGEFEERL KAVLEEIKAS DGQVITFIDE LHTVVGAGAT GDSAMDAGNM
     LKPMLARGEL RMIGATTLDE YRENVEKDPA LERRFQQVLV GEPSVEDTIA ILRGLKERYE
     AHHKVAIADA ALVAAATLSD RYIPGRQLPD KAIDLVDEAG SRLRMEIDSS PVEIDELRRA
     VDRLRMEELH LQNETDDASR ERLEKLRSEL ADRQETLRAL EQRWESEKQS LNAVGEIKER
     IDEVRIAAER AQREGDLETA ARLLYSEIPT MEAQLAAAQA AESAREAGDG TDRLVNEEVT
     ADEIAEVVAS WTGIPTGRLL EGETGKLLRM EDELGKRLVG QREAVTAVSD AVRRSRAGIA
     DPDRPTGSFL FLGPTGVGKT ELAKTLAEFL FDDERAMVRI DMSEYAEKHA VSRLVGAPPG
     YVGYDEGGQL TEAVRRRPYS VVLLDEVEKA HPEVFDILLQ VLDDGRLTDG QGRTVDFRNV
     ILILTSNLGS VFLADPSLDE QAKKDAVMDV VKASFKPEFL NRLDEIVTFE PLGTAELTHI
     VDLQLASLGR RLAARRITLD VTDAAKEWLA LTGWDPAYGA RPLRRLVQQA IGDRLAKALL
     AGEVRDGDTV RVDREVGPDG VPTDSLTVTA A
//
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