GenomeNet

Database: UniProt
Entry: A0A0F7FV05_9ACTN
LinkDB: A0A0F7FV05_9ACTN
Original site: A0A0F7FV05_9ACTN 
ID   A0A0F7FV05_9ACTN        Unreviewed;       861 AA.
AC   A0A0F7FV05;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SXIM_28650 {ECO:0000313|EMBL:AKG44249.1};
OS   Streptomyces xiamenensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG44249.1, ECO:0000313|Proteomes:UP000034034};
RN   [1] {ECO:0000313|Proteomes:UP000034034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA   Xu J.;
RT   "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL   Submitted (FEB-2015) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP009922; AKG44249.1; -; Genomic_DNA.
DR   RefSeq; WP_030733039.1; NZ_CP009922.3.
DR   AlphaFoldDB; A0A0F7FV05; -.
DR   STRING; 408015.SXIM_28650; -.
DR   KEGG; sxi:SXIM_28650; -.
DR   PATRIC; fig|408015.6.peg.2901; -.
DR   HOGENOM; CLU_005070_4_1_11; -.
DR   Proteomes; UP000034034; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..152
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          409..489
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   861 AA;  94206 MW;  5EE8D2710A62996C CRC64;
     MSAELTNRSR EAISGANDRA LTEGHSDITP AHLLLALLEG QDNENIRDLL ASVGADAAAL
     RAGAERLLGA LPTVQGSTVS RPQPNRELMA VLADAGRRAT DLGDTFVSTE HLLIGIADRG
     GKAGEPLDAK ALADAFQRSR GAQRVTTADP ENTYKALEKY GTDFTAAARE GKLDPVIGRD
     HEIRRVVQVL SRRTKNNPVL IGEPGVGKTA VVEGLAQRMV KGDVPESLRN KRLVSLDLGA
     MVAGAKYRGE FEERLKAVLA EIKSSDGQIV TFIDELHTVV GAGAGGDSAM DAGNMLKPML
     ARGELRMVGA TTLDEYRERI EKDAALERRF QQVLVAEPTV EDSIAILRGL KGRYEAHHKV
     QIADAALVAA ATLSDRYITS RFLPDKAIDL VDEAASRLRM EIDSSPVEID ELQRSVDRLR
     MEELALANES DATSKERLAR LRRELADREE ELRGLTARWE KEKQGLNRVG ELKERLDETR
     GQAERAQRDG DFETASKLLY AEIPALEREL ADAAEAEQET AARATMVKEE VGPDDIADVV
     SSWTGIPAGR LLEGETEKLL RMEEELGRRL IGQTDAVRAV SDAVRRSRAG VADPDRPTGS
     FLFLGPTGVG KTELAKALAD FLFDDERAMV RIDMSEYSEK HSVARLVGAP PGYVGYEEGG
     QLTEAVRRRP YTVVLLDEVE KAHHEVFDIL LQVLDDGRLT DGQGRTVDFR NTILILTSNL
     GSQHLMDPLA KPHERREQVL AAVRAAFRPE FLNRLDDLVV FSALDISELS RIARLQIDSL
     QRRLADRRLT LEITEPALHW LAEEGLDPAY GARPLRRLVQ TAIGDQLARR ILAGEVRDGD
     TVRVEPSAEG GGLLVSAVPA G
//
DBGET integrated database retrieval system