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Database: UniProt
Entry: A0A370BAD7_9ACTN
LinkDB: A0A370BAD7_9ACTN
Original site: A0A370BAD7_9ACTN 
ID   A0A370BAD7_9ACTN        Unreviewed;       868 AA.
AC   A0A370BAD7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RDG36405.1};
GN   ORFNames=DVH02_20195 {ECO:0000313|EMBL:RDG36405.1};
OS   Streptomyces corynorhini.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG36405.1, ECO:0000313|Proteomes:UP000253741};
RN   [1] {ECO:0000313|EMBL:RDG36405.1, ECO:0000313|Proteomes:UP000253741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC230 {ECO:0000313|EMBL:RDG36405.1,
RC   ECO:0000313|Proteomes:UP000253741};
RA   Dunlap C.;
RT   "Streptomyces species from bats.";
RL   Submitted (JUL-2018) 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:RDG36405.1}.
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DR   EMBL; QQNA01000158; RDG36405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370BAD7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000253741; 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:UP000253741};
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..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   868 AA;  94771 MW;  CAACA1D540697EB2 CRC64;
     MDAELTNKSR DAINAATSRA VAAGHPDLTP AHLLLALLEG QDNENVTDLL AAVEADQASV
     RAGAERLLAA EPSVTGSTVA PPQPNRELLA VIADAARRAK ELGDEYVSTE HVLIGIAAKG
     GQAGTVLAER GAAAEKLLGA FETARGGRRV TTADPEGQYK ALEKFGTDFT AAAREGKLDP
     VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLRNKRLVS
     LDLGAMVAGA KYRGEFEERL KTVLSEIKDS DGQIVTFIDE LHTVVGAGAG GDSAMDAGNM
     LKPMLARGEL RMVGATTLDE YRERIEKDAA LERRFQQVLV AEPSVEDTIA ILRGLKGRYE
     AHHKVQIADA ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRS
     VDRLRMEELA LKNESDPASK QRLEKLRRDL ADRDEELRGL NARWQKEKQG LNRVGELKER
     LDELRGQAER AQRDGDFDTA SKLLYGEIPG LERELEEASE AEQEAAKDTM VKEEVGPDDI
     ADVVGSWTGI PAGRLLEGET QKLLRMEQEL GRRLIGQSEA VEAVSDAVRR TRAGIADPDR
     PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YGEKHSVARL VGAPPGYVGY
     EEGGQLTEAI RRRPYSVVLL DEVEKAHPEV FDVLLQVLDD GRLTDGQGRT VDFRNTILVL
     TSNLGSQYLV DPLTSPERKK EQVLQTVRSS FKPEFLNRLD DLVVFSALSR DELAHIAGLQ
     IERLAKRLAE RRLTLDVTPA ALEWLADEGN DPAYGARPLR RLVQTAIGDR LAKEILAGEV
     TDGDTVRVDR FEDGLIVGTA PTSLEKTP
//
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