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Database: UniProt
Entry: A0A2T0MD03_9FLAO
LinkDB: A0A2T0MD03_9FLAO
Original site: A0A2T0MD03_9FLAO 
ID   A0A2T0MD03_9FLAO        Unreviewed;       850 AA.
AC   A0A2T0MD03;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:PRX55381.1};
GN   ORFNames=CLV81_3793 {ECO:0000313|EMBL:PRX55381.1};
OS   Allomuricauda pacifica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1080225 {ECO:0000313|EMBL:PRX55381.1, ECO:0000313|Proteomes:UP000237640};
RN   [1] {ECO:0000313|EMBL:PRX55381.1, ECO:0000313|Proteomes:UP000237640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25027 {ECO:0000313|EMBL:PRX55381.1,
RC   ECO:0000313|Proteomes:UP000237640};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-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:PRX55381.1}.
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DR   EMBL; PVYX01000002; PRX55381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0MD03; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000237640; 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:PRX55381.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PRX55381.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..149
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          148..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          444..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        148..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  95750 MW;  0C13EDD2C4BB9C58 CRC64;
     MDDNFSPRVK DVIAYSKEEA LRLGHDFIGT EHLMLGLLRD GNGKAINILD ALDVDLDHLR
     RKVEILSPAN PNTGTIQKDK KNLHLTRQAE RALKTTFLEA KLFQSSSINT AHLLLCILRN
     ENDPTTKLLH KLKVDYDNVK EQFKSMITSE DDYLDTPRAE SFPSDPEETG ESKESGFGGS
     SSQKGSKKSK TPVLDNFGRD LTRLAEENKL DPVVGREKEI ERVSQILSRR KKNNPLLIGE
     PGVGKSAIAE GLALRIINKK VSRILYNKRV VTLDLASLVA GTKYRGQFEE RMKAVMNELE
     KNDDIILFID EIHTIVGAGG ATGSLDASNM FKPALARGEI QCIGATTLDE YRQYIEKDGA
     LERRFQKVMV EPTTVEETIE ILMNIKGKYE DHHNVNYTDN AIVACVKLTN RYMTDRFLPD
     KAIDALDEAG SRVHIVNMDV PKQILELETQ LEDVRELKNS VVKKQKYEEA AKLRDDEKRL
     EKELMAAQER WEAESKMHRE TVSEENVADV VSMMSGIPVN RIAQTESNKL AELPELIKGF
     VIGQDEAVAK VAKAIQRNRA GLKDPNKPIG SFIFLGQTGV GKTQLAKILA KELFDSEDAL
     IRIDMSEYME KFAISRLVGA PPGYVGYEEG GQLTEKVRRK PYSVILLDEV EKAHPDVFNM
     LLQVLDDGYL TDSLGRKIDF RNTIIIMTSN IGARQLKDFG QGVGFGTAAK KAQADTHQKS
     VIENALKKAF APEFLNRIDD VIVFNPLERE DIHKIIDIEL DKLFKRIKDI GYDLNLSEKA
     KDYIAEKGFD KQYGARPLKR AIQKYIEDAL AEEIVNSKLE EGDSIFMDLD EKKEELTIKI
     KKPKKSQEAE
//
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