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Database: UniProt
Entry: A0A164IVQ1_9NOCA
LinkDB: A0A164IVQ1_9NOCA
Original site: A0A164IVQ1_9NOCA 
ID   A0A164IVQ1_9NOCA        Unreviewed;       851 AA.
AC   A0A164IVQ1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AWN90_07165 {ECO:0000313|EMBL:KZM69791.1};
OS   Nocardia terpenica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM69791.1, ECO:0000313|Proteomes:UP000076512};
RN   [1] {ECO:0000313|EMBL:KZM69791.1, ECO:0000313|Proteomes:UP000076512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM69791.1,
RC   ECO:0000313|Proteomes:UP000076512};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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:KZM69791.1}.
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DR   EMBL; LWGR01000017; KZM69791.1; -; Genomic_DNA.
DR   RefSeq; WP_067578763.1; NZ_KV411303.1.
DR   AlphaFoldDB; A0A164IVQ1; -.
DR   STRING; 455432.AWN90_07165; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000076512; 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:UP000076512};
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          413..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   851 AA;  93001 MW;  4B95C54F5237B7E0 CRC64;
     MDSFNPTTKT QAALTAALQA ASAAGNPEIR PAHLLVALLD QTDGIAAPLL KAAAVDPATV
     RREAQDIVDR LPRATGATTT PQLGREALAA ITAAQKLATE LGDEYVSTEH LMVGLAAGDS
     DVSQLLLKYG ATADALREAF TTVRGNARVT GPDPEGSYQA LEKYSTDLTA AAREGKLDPV
     IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRGKRLVSL
     DLGAMVAGAK YRGEFEERLK AVLEEIKTSA GQIITFIDEL HTIVGAGATG ESAMDAGNMI
     KPMLARGELR LVGATTLDEY RQHIEKDPAL ERRFQQVLVG EPSVEDTIGI LRGLKERYEV
     HHGVRITDSA LVAAATLSDR YITSRFLPDK AIDLVDESAS RLRMEIDSRP VEIDEVERAV
     RRLEIEEMAL AKETDEASKQ RLEKLRQELA DDREKLNQLM ARWQNEKQAI DAVRVVKEQL
     EALKGESERA ERDGDLGKAA ELRYGRIPQL EKQLAEAERK AGTAADGEVM LQEEVGPNDI
     AEVVSAWTGI PVGRMLEGET QKLLRMEDEL GKRVVGQKEA VQAVSDAVRR ARAGVADPNR
     PTGSFMFVGP TGVGKTELAK ALADFLFDDE RAMIRIDMSE YSEKHSVARL VGAPPGYVGY
     DQGGQLTEAV RRRPYTVVLF DEIEKAHPDV FDILLQVLDE GRLTDGQGRT VDFRNTILIL
     TSNLGAGGDR DQIMNAVRGA FKPEFLNRLD DVVMFHALNE EQLEDIVDIQ LNQLQKRLSQ
     RRLKLDVSDS ARFWLAVRGY DPVYGARPLR RLIQQAIGDS LAKELLAGEV TDGDLVKVNV
     SPDGDGLIVG R
//
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