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
//