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Database: UniProt
Entry: A0A2B8AWX8_9ACTN
LinkDB: A0A2B8AWX8_9ACTN
Original site: A0A2B8AWX8_9ACTN 
ID   A0A2B8AWX8_9ACTN        Unreviewed;       911 AA.
AC   A0A2B8AWX8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=ATP-dependent chaperone ClpB {ECO:0000313|EMBL:PGH49562.1};
GN   ORFNames=CRI70_16920 {ECO:0000313|EMBL:PGH49562.1};
OS   Streptomyces sp. Ru87.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2044307 {ECO:0000313|EMBL:PGH49562.1, ECO:0000313|Proteomes:UP000222409};
RN   [1] {ECO:0000313|EMBL:PGH49562.1, ECO:0000313|Proteomes:UP000222409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru87 {ECO:0000313|EMBL:PGH49562.1,
RC   ECO:0000313|Proteomes:UP000222409};
RA   Amin D.H., Borsetto C., Abolmaaty A., Tolba S., Abdallah N.A.,
RA   Wellington E.M.H.;
RT   "Draft genome sequence of Streptomyces sp. Ru87 isolated from Egyptian
RT   soil.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
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:PGH49562.1}.
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DR   EMBL; PDIX01000269; PGH49562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B8AWX8; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000222409; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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   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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222409};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          433..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   911 AA;  99406 MW;  F3216CE4A1B8D015 CRC64;
     MDAELTNRSQ EAISAAGRRA VSAGNPDITP AHLLLALIEG QENENIQDLL AAVEADQASL
     RSAAERLLGA LPSVQGSTVA PPQPDRELLA VAADASRRAK ELGDAYISTE HLLIGLAAKG
     GQTGEILSQQ GASAEKLLDA FETTRGGRRV TTPDPEGTYK ALEKFGTDFT AIAREGKLDP
     VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKNKRLVA
     LDIGAMLAGA KYRGEFEERL KTVLSEIKES DGQIITFIDE LHTVVGAGAG GDSAMDAGNM
     LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV SEPDVQDSIA ILRGLKGRYE
     AHHGVQIADS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLQMEIDSS PVEIDELQRA
     VDRQMMEEES LLAAHSDDAQ GGKNLLRKKK DREQDLSPDA RERLDRLRKE RAEKEEKLRA
     LRARWDSEKA IHTRVGELKK RLDELETELE LAERKAPETG DWVTPGRLRS EVIPATRKQL
     DAAAEEQKSL QGSGMVGEEV GPDDIADVVA AWTGIPAGRM LEGETQKLLR MEDELGKRLI
     GQTEAVRAVS DAVRRTRAGI SDPDRPTGSF LFLGPTGVGK TELAKALADF LFDDERAMVR
     IDMSEYSEKH SVARLVGAPP GYVGYEEGGQ LTEAVRRRPY SVVLLDEVEK AHHEVFDILL
     QVLDDGRLTD GQGRTVDFRN TILVLTSNLG SHYLVDPSIG EEKKRERVLE TVRSSFRPEF
     LNRLDDLVVF HALGTEQLKR IARLQLGLLQ RRLADRRLTL DVTDAALEWL SRLGQEPVID
     APEEAGPDLS YGARPLRRLV QTAIGDQLAR AILAGDVADG DTVRVDVSED GRRLTVAASG
     PAGALESAAG A
//
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