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Database: UniProt
Entry: A0A6I4MQL4_9ACTN
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ID   A0A6I4MQL4_9ACTN        Unreviewed;       844 AA.
AC   A0A6I4MQL4;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=AAA domain-containing protein {ECO:0000313|EMBL:MWA08448.1};
GN   ORFNames=E5671_04530 {ECO:0000313|EMBL:MWA08448.1};
OS   Streptomyces sp. BA2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=436595 {ECO:0000313|EMBL:MWA08448.1, ECO:0000313|Proteomes:UP000431136};
RN   [1] {ECO:0000313|EMBL:MWA08448.1, ECO:0000313|Proteomes:UP000431136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA2 {ECO:0000313|EMBL:MWA08448.1,
RC   ECO:0000313|Proteomes:UP000431136};
RA   Ince E.;
RT   "Complete genome sequence of Streptomyces sp. BA2.";
RL   Submitted (DEC-2019) 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:MWA08448.1}.
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DR   EMBL; WSRO01000002; MWA08448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6I4MQL4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000431136; 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; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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   InterPro; IPR001943; UVR_dom.
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.
DR   PROSITE; PS50151; UVR; 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|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000431136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          33..181
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          448..483
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          158..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          444..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        163..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  91721 MW;  B343C16C7B01C110 CRC64;
     MSSGFPGPEG FGQDPFGELF ARFFGNGRRQ IDIGRLMSGP ARQLVTTAAS YAADHGQSNL
     DTEHLLRAAL TLEPTRGLIE RSGADPETIA AEIDRHAGEA GGVTAPQAVA LTPAVKRALL
     DAHDVARAVG AGYIGPEHIV MALAANPDSA AGHILNAARF DPGSTPQAPQ GQPGTAEPRQ
     QGSGGATPTL DQYGRDLTAL AGEGRVDPVI GREEEIEQTI EVLSRRGKNN PVLIGDAGVG
     KTAVVEGLAQ RIVDGDVPET LADRRVIALD LAGVVAGTRY RGDFEERLNG IINEVRAHSD
     EVIVFIDELH TVVGAGGGGS EGGSMDAGNM LKPALARGEL HVIGATTLEE YRRYIEKDAA
     LARRFQPILV SEPTAADAVE ILRGLRDRYE AHHQVRYSDQ ALLAAVELSD RYLTERFLPD
     KAIDLMDQAG ARVRLRSRTK GTDVRALERE MEQAVRDKDQ AVAAENYERA TELRDRISEL
     ARKIEAGQTR EPGDGQIVEV APDDIAEVVS RQTGIPVSTL TQEEKERLLG LEQHLHERVV
     GQDEAVSAVA EAVLRSRSGL SSPDRPIGSF LFLGPTGVGK TELARALAEA LFGSEERMVR
     LDMSEFQERH TVSRLVGAPP GYVGHEEAGQ LTEAVRRHPY SLLLLDEVEK AHPDVFNILL
     QVLDDGRLTD AQGRTVNFTN TVIVMTSNLG SEAITGRGAA LGFRADGSDS DEEARREQVL
     RPLREHFRPE FLNRIDEVVI FRRLSGEQLR QVTDLLLEET RRRLHAQDIT IDFSPAAVDW
     LAQRGHQPEY GARPLRRTIQ REVDNRLSRL LLDGQLAAGS RALVDVDDDA LTIRPAQDAT
     PREA
//
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