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Database: UniProt
Entry: A0A1I5U690_9BACT
LinkDB: A0A1I5U690_9BACT
Original site: A0A1I5U690_9BACT 
ID   A0A1I5U690_9BACT        Unreviewed;       842 AA.
AC   A0A1I5U690;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SFP90793.1};
GN   ORFNames=SAMN05444277_10395 {ECO:0000313|EMBL:SFP90793.1};
OS   Parafilimonas terrae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Parafilimonas.
OX   NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFP90793.1, ECO:0000313|Proteomes:UP000199031};
RN   [1] {ECO:0000313|EMBL:SFP90793.1, ECO:0000313|Proteomes:UP000199031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28286 {ECO:0000313|EMBL:SFP90793.1,
RC   ECO:0000313|Proteomes:UP000199031};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; FOXQ01000003; SFP90793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5U690; -.
DR   STRING; 1465490.SAMN05444277_10395; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199031; 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:SFP90793.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFP90793.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199031};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          441..476
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          147..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..483
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   842 AA;  95376 MW;  13CA1363C78DD91F CRC64;
     MDNNFSAQVK EIISYSREEA LRLGNDFIGT EHLLLGLIRD GENTAIKILK QLNVDLYELR
     KEVELAVRDK TGKNIANINS IPLTKQAEKV IRVTVLEAKA LKSPLVETEH LMLSILKNKE
     NIATQILNQY DVDYDLFKTE LGVVRSNEPR SEYTEENDDD FEDERKQGYS SAQKKTTGNA
     KSKTPVLDNF GRDITKLAET GALDPIVGRE KEIERVSQIL SRRKKNNPIL IGEPGVGKTA
     IVEGLALRIV QRKVSRVLYD KRVISLDLAA LVAGTKYRGQ FEERMKAIMN ELEKNRDVIL
     FIDEIHTIVG AGGASGSLDA SNIFKPALSR GELQCIGAST LDEYRMYIEK DGALDRRFQK
     VIVDPPTVEE TIQILNNIKP RYEDYHNVVY SNDAIEACVK LSDRYMTDRL LPDKAIDVLD
     EVGARVHLKN INVPQNILDL EKQIEEIKLE KNRVVKSQRF EEAAALRDTE KRLGEELEKA
     KTDWEEESKH KRYPIDEENI AEVVSMMTGI PVKRMVQAES EKLRKMSEDM RGMVIGQDEA
     ISKVVKAIQR NRVGLKDPKK PVGSFIFLGP TGVGKTELAR SLARYMFDSE DALIRIDMSE
     YMEKFTVSRL IGAPPGYVGY EEGGQLTEKV RRKPYCVILL DEIEKAHPDI YNILLQVLDD
     GQLTDGLGRK VDFKNTLIIM TSNIGVRQLK DFGEGVGFAT AARVQSAEEN NKAVIEKALK
     RTFSPEFLNR IDDVVIFNSL SKENIFQIID ILMKGVLKRL NNMGFTLEIT NEAKEFIAEK
     GYDVQFGARP LHRAIQKYLE DSLAEEILNM NIKQGDVLIA DLDKENQKIK FEFGKKEEEA
     KV
//
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