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Database: UniProt
Entry: A0A495KLI3_9FLAO
LinkDB: A0A495KLI3_9FLAO
Original site: A0A495KLI3_9FLAO 
ID   A0A495KLI3_9FLAO        Unreviewed;       847 AA.
AC   A0A495KLI3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:RKS02291.1};
GN   ORFNames=C8C84_2000 {ECO:0000313|EMBL:RKS02291.1};
OS   Flavobacterium sp. 102.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2135623 {ECO:0000313|EMBL:RKS02291.1, ECO:0000313|Proteomes:UP000270484};
RN   [1] {ECO:0000313|EMBL:RKS02291.1, ECO:0000313|Proteomes:UP000270484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=102 {ECO:0000313|EMBL:RKS02291.1,
RC   ECO:0000313|Proteomes:UP000270484};
RA   Chistoserdova L.;
RT   "Synthetic bacterial communities of pure cultures isolated from sediment of
RT   Lake Washington, USA.";
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:RKS02291.1}.
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DR   EMBL; RBKX01000001; RKS02291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495KLI3; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000270484; 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:RKS02291.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RKS02291.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          447..482
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          443..489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        153..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  95338 MW;  3596B026C7F8A44D CRC64;
     MDDNFSPRVK DVITYSKEEA LRLGHDFIGT EHLMLGILRD GNGKAIAILN NLSIDLEHLR
     KKVEILSPAN PNVEISNEKK NLHLTRQAER ALKTTFLEAK VFQATSISTA HLLLCILRNE
     NDPTTKLLHR LKIDYNVVKE QYLNMTPNEE DFTDNLPRNE SFNDDSGQDD SLKEGSFNNP
     ANKTNKKSKT PVLDNFGRDL TELAEEGKLD PVVGREKEIE RVSQILSRRK KNNPLLIGEP
     GVGKSAIAEG LALRIIQKKV SRILFNKRVV TLDLASLVAG TKYRGQFEER MKAVMNELEK
     NDDIILFIDE IHTIVGAGGA TGSLDASNMF KPALARGEIQ CIGATTLDEY RQYIEKDGAL
     ERRFQKVIVE PTSVEETITI LNNIKNKYED HHNVIYTDEA IEACVKLTNR YMSERFLPDK
     AIDALDEAGS RVHITNIDVP KQILDLERQL EEVRDLKNSV VKKQKYEEAA KLRDDEKRLE
     KDLAIAQEQW EEDSKNNRIR VTEDNVADVV SMMTGIPVNR IAQTESNKLA HLPELIQGKV
     IGQNDAVLKI SRSIQRNRAG LKDPNRPIGS FIFLGQTGVG KTQLAKVLAK ELFDSEDALI
     RIDMSEYMEK FAISRLIGAP PGYVGYEEGG QLTEKVRRKP YCVVLLDEIE KAHPDVFNMM
     LQVLDDGYLT DSLGRKIDFK NTIIIMTSNV GARQLKDFGQ GVGFGTAAKV AQADDHSKSV
     VENALKKTFA PEFLNRIDDV IVFNPLEKHD IDLIIEIELK KLFARVEELG YKLNLSDTAK
     AFIAEKGFDK QFGARPLKRA IQKYVEDALA EEIITSKIAS GDEIFMDLDE ASQELTVTIQ
     KAEKPTK
//
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