ID A0A076N228_AMYME Unreviewed; 867 AA.
AC A0A076N228;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:AIJ26888.1};
GN ORFNames=AMETH_6796 {ECO:0000313|EMBL:AIJ26888.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ26888.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ26888.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ26888.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL Submitted (JUL-2014) 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}.
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DR EMBL; CP009110; AIJ26888.1; -; Genomic_DNA.
DR RefSeq; WP_017985662.1; NZ_CP009110.1.
DR AlphaFoldDB; A0A076N228; -.
DR STRING; 1068978.AMETH_6796; -.
DR KEGG; amq:AMETH_6796; -.
DR PATRIC; fig|1068978.7.peg.7300; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_11; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000062973; 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 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:UP000062973};
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 COILED 414..501
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 93990 MW; F2651DBDFA060233 CRC64;
MDAFNPTTKT QQAISSAAQA ATVAGNPSVT AAHLLGALLA QGDGLAGPLL TAVGADPRQV
HKELEPITQG LPSATGATVS TPQFDPPAVK SLTHAQKLAT ELGDEYVSTE HLMVGLAAEG
GQVADLLKRH GATPDALREA FTKVRGSARI TSPDPEGTFK ALEKYGVDLT DRARKGELDP
VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVAGDVP ESLRGKRVVA
LDLGSMVAGA KYRGEFEERL KAVLKEITES AGQVITFIDE LHTIVGAGAT GEGAMDAGNM
IKPMLARGEL RMVGATTLDE YRQHIEKDAA LERRFQQVLV GEPSVEDTIG ILRGLKERYE
VHHGVRITDA ALVSAATLSD RYITARFLPD KAIDLVDEAA SRLRMEIDSR PVEIDEVERA
VRRLEIEEMA LSKEEDPASV ERLAALRAEL AEKREELSAL TARWQNEKGS IEKVRELKEQ
LEQLRGEADR AERDADLGRA AELRYGKIPA LEKDLEAAQR NTATSSSGAD VMLKEEVGAD
DVADVVSAWT GIPAGRLLEG ETGKLLRMEE ELGKRVVGQR EAVQAVSDAV RRTRAGVADP
DRPTGSFLFL GPTGVGKTEL AKALAEFLFD DERAMTRIDM SEYSEKHSVA RLVGAPPGYV
GYDQGGQLTE AVRRRPYSVV LLDEVEKAHP DVFDVLLQVL DDGRLTDGQG RTVDFRNTIL
VLTSNLGSQA IADASLDEQQ RRDAVLSTVQ RHFKPEFLNR LDDIVVFHSL DTEQLTSIVD
IQVAKLATRL AQRRLTLDVT PGARDWLALN GFDPIYGARP LRRLVQSAIG DQLAKKLLAG
EVRDGDTVRV DVPDLNAGDT LVVTRAD
//
