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Database: UniProt
Entry: A0A3M0G3W9_9FLAO
LinkDB: A0A3M0G3W9_9FLAO
Original site: A0A3M0G3W9_9FLAO 
ID   A0A3M0G3W9_9FLAO        Unreviewed;       853 AA.
AC   A0A3M0G3W9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:RMB59535.1};
GN   ORFNames=EAX61_08095 {ECO:0000313|EMBL:RMB59535.1};
OS   Dokdonia sinensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Dokdonia.
OX   NCBI_TaxID=2479847 {ECO:0000313|EMBL:RMB59535.1, ECO:0000313|Proteomes:UP000281985};
RN   [1] {ECO:0000313|EMBL:RMB59535.1, ECO:0000313|Proteomes:UP000281985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH27 {ECO:0000313|EMBL:RMB59535.1,
RC   ECO:0000313|Proteomes:UP000281985};
RA   Zhou L.Y., Du Z.J.;
RT   "Dokdonia luteus sp. nov., isolated from sea water.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {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:RMB59535.1}.
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DR   EMBL; REFV01000006; RMB59535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0G3W9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000281985; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:RMB59535.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RMB59535.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281985};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          451..486
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          155..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          466..493
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        155..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  95529 MW;  C84DE183F6CEA011 CRC64;
     MDDNFSPRVK DVIAYSKEEA LRLGHDFIGT EHLLLGLLRD GSGKAIDILG ALDIDLEHLR
     RKVEILSPAN PNIALQGNDK KNLHLTRQAE RALKTTFLEA KLFQSSSINT AHLLLCVLRN
     ENDPTTKLLN KLKVDYDNVK DQFKVMMSSE DENYIEPIKS ESFSEDETSG DDASKDNPFS
     APSGNKGATK KSKTPVLDNF GRDLTTMAEE DKLDPVVGRG KEIERVSQIL SRRKKNNPLL
     IGEPGVGKSA IAEGLALRIV QRKVSRILFD KRVVTLDLAS LVAGTKYRGQ FEERMKAVMN
     ELEKNDDIIL FIDEIHTIVG AGGATGSLDA SNMFKPALAR GEIQCIGATT LDEYRQYIEK
     DGALERRFQK VIVEPTSVEE TIEILDNIKG KYEEHHNVTY TDEAIKACVT LTNRYMTDRF
     LPDKAIDALD EAGSRVHITN IDVPKKILEL EGQLEQVREL KTSVVKKQKY EEAAKLRDDE
     KKIEKELATA QKQWEDDAKL HKEEVSEDNV ADVVSMMTGI PVNRIAQTES NKLAELPATI
     KTKVIGQDDA VAKVAKAIQR NRAGLKDPNK PIGSFIFLGQ TGVGKTQLAK VLAKELFDNE
     DSLIRIDMSE YMEKFAISRL VGAPPGYVGY EEGGQLTEKV RRKPYSVILL DEIEKAHPDV
     FNMMLQVLDD GFLTDSLGRK IDFRNTIIIM TSNIGARKLK DFGQGVGFGT ASRKTQSDEN
     ARSIIQNALK KAFAPEFLNR IDDVVVFNAL EREDIHKIID IELAKLYSRI KGLGYDLSLS
     EKAKDYISDK GFDKEYGARP LKRAIQKYIE DALAEEIITS NLEEGDAIFM DFDEKEDELT
     IKISKQEQPS ESK
//
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