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}.
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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
//