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Database: UniProt
Entry: A0A250VFP8_STROL
LinkDB: A0A250VFP8_STROL
Original site: A0A250VFP8_STROL 
ID   A0A250VFP8_STROL        Unreviewed;       861 AA.
AC   A0A250VFP8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:GAX53007.1};
GN   ORFNames=SO3561_04532 {ECO:0000313|EMBL:GAX53007.1};
OS   Streptomyces olivochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1963 {ECO:0000313|EMBL:GAX53007.1, ECO:0000313|Proteomes:UP000217446};
RN   [1] {ECO:0000313|Proteomes:UP000217446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3561 {ECO:0000313|Proteomes:UP000217446};
RA   Dohra H., Kodani S.;
RT   "Streptomyces olivochromogenes NBRC 3561 whole genome shotgun sequence.";
RL   Submitted (MAY-2017) 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:GAX53007.1}.
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DR   EMBL; BDQI01000009; GAX53007.1; -; Genomic_DNA.
DR   RefSeq; WP_067374176.1; NZ_KQ948460.1.
DR   AlphaFoldDB; A0A250VFP8; -.
DR   STRING; 1963.AQJ27_27100; -.
DR   Proteomes; UP000217446; 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:UP000217446};
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   861 AA;  94193 MW;  B666C701B8395EB1 CRC64;
     MDAELTNRSR DAINAATSRA VSEGHPDLTP AHLLLALLGG QENENITDLL AAVDADQAAV
     RAGAERVLAG LPSVTGSTVA PPQPNRELLA VIAEAADKAK ELGDEYLSTE HLLIGIAAKG
     GPSGDVLSQQ GASAKKLLEA FQKSRGGRRV TTPDPEGQYK ALEKFGTDFT AAAREGKLDP
     VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKNKRLVS
     LDLGAMVAGA KYRGEFEERL KTVLAEIKDS DGQIITFIDE LHTVVGAGAG GDSAMDAGNM
     LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPSVEDTIA ILRGLKGRYE
     AHHKVVIADS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRA
     VDRLRMEELA LDKETDPASR QRLEKLRRDL ADKEEELRGL TARWEKEKQS LNRVGELKEK
     LDELRGQAER AQRDGDFDTA SKLLYGEIPT LERDLEEASE AEEEAARDTM VKEEVGPDDI
     ADVVGSWTGI PAGRLLEGET QKLLRMEEEL GRRLIGQSEA VQAVSDAVRR TRAGIADPDR
     PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMIRIDMSE YGEKHSVARL VGAPPGYIGY
     EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNTILIL
     TSNLGSQFLV EPLTSEEEKK QQVLEVVRAS FKPEFLNRLD DLVVFSALNM EELERIARLQ
     VDRLAKRLAQ RRITLEVTDA ALAWLADEGN DPAYGARPLR RLVQTAIGDR LAKEILAGEV
     KDGDTVRVDA FGDGLIVGAA Q
//
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