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Database: UniProt
Entry: A0A328WQG8_9FLAO
LinkDB: A0A328WQG8_9FLAO
Original site: A0A328WQG8_9FLAO 
ID   A0A328WQG8_9FLAO        Unreviewed;       849 AA.
AC   A0A328WQG8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:RAR48602.1};
GN   ORFNames=B0I10_105218 {ECO:0000313|EMBL:RAR48602.1};
OS   Flavobacterium lacus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1353778 {ECO:0000313|EMBL:RAR48602.1, ECO:0000313|Proteomes:UP000249518};
RN   [1] {ECO:0000313|EMBL:RAR48602.1, ECO:0000313|Proteomes:UP000249518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12504 {ECO:0000313|EMBL:RAR48602.1,
RC   ECO:0000313|Proteomes:UP000249518};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-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:RAR48602.1}.
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DR   EMBL; QLSV01000005; RAR48602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328WQG8; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000249518; 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:SF193; CHAPERONE PROTEIN CLPB; 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:RAR48602.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RAR48602.1};
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          449..484
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          148..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          445..491
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..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  95508 MW;  1A1A74A674A08DB9 CRC64;
     MDDNFSPRVK DVITYSKEEA LRLGHDFIGT EHLMLGILRD GNGKAITILS NLDIDLDYLR
     KKVEILSPPN PNAEVGNEKK NLHLTRQAER ALKTTFLEAK VFQSSSISTA HLLLCILRNE
     NDPTTKLLNK LKIDYDIAKE QYLNMIPNNN EDEYTDSFPK NESFNEDSGQ DDSLKEGNFN
     NPASKTNKKS KTPVLDNFGR DLTEMAEEGK LDPVVGREKE IERVSQILSR RKKNNPLLIG
     EPGVGKSAIA EGLALRIIQK KVSRILFNKR VVTLDLASLV AGTKYRGQFE ERMKAVMNEL
     EKNDDIILFI DEIHTIVGAG GATGSLDASN MFKPALARGE IQCIGATTLD EYRQYIEKDG
     ALERRFQKVI VEPTSIEETI TILNNIKGKY EDHHSVTYTQ EAIDACVKLT SRYMSDRFLP
     DKAIDALDEA GSRVHITNIE VPKQILELEK QLEDVRELKN TVVKKQKYEE AAKLRDDEKR
     IEKDLAIAQE QWEIDSKNNR ITVTEDNVAD VVSMMTGIPV NRIAQTESNK LAHLPELIRG
     KVIGQDEAVM KIARSIQRNR AGLKDPNRPI GSFIFLGQTG VGKTQLAKVL AKELFDSEDA
     LVRIDMSEYM EKFAISRLVG APPGYVGYEE GGQLTEKVRR KPYCVVLLDE IEKAHPDVFN
     MMLQVLDDGY LTDSLGRKID FRNTIIIMTS NVGARQLKDF GQGVGFGTAA KVSQADDHSK
     SVIENALKKT FAPEFLNRID DVIVFNALEK EHIDLIIEIE LKKLYARIKD LGYTLNLSDK
     AKAFIAEKGF DKQFGARPLK RAIQKYVEDS LAEEIITSKI GEGDEIFMDI EDDAQELNVK
     IQKAEKPTS
//
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