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
//