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Database: UniProt
Entry: A0A1W6E888_9BACT
LinkDB: A0A1W6E888_9BACT
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ID   A0A1W6E888_9BACT        Unreviewed;       844 AA.
AC   A0A1W6E888;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:ARK11644.1};
GN   ORFNames=A6C57_15645 {ECO:0000313|EMBL:ARK11644.1};
OS   Fibrella sp. ES10-3-2-2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK11644.1, ECO:0000313|Proteomes:UP000193660};
RN   [1] {ECO:0000313|Proteomes:UP000193660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA   Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL   Submitted (APR-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; CP015317; ARK11644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6E888; -.
DR   STRING; 1834519.A6C57_15645; -.
DR   KEGG; fib:A6C57_15645; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000193660; Chromosome.
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:ARK11644.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ARK11644.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193660};
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          444..479
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          146..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          440..490
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   844 AA;  93971 MW;  8E130FCEBE5F2128 CRC64;
     MEAKFSNRVK EVISLSREEA LRLGHDYIGT EHLLLGMIRE GEGVAVGLLK KLSISLDELR
     ITIEQATKGT ATNNVKNLAN IPLTRQSEKT LKITYLEAKI FKSPLIGTEH LLLSILRDED
     NVATQILHKF NVNYEVIKEM LEYQSTGTQP NMAHDTDDDD DASRGMFGGG GSGTGQGKEK
     GSEKSRTPVL DNFGRDLTKL AEVGKLDPIV GREKEIERVA QILSRRKKNN PILIGEPGVG
     KTAIAEGLAL RIVQKKVSRV LFGKRVVTLD LASLVAGTKY RGQFEERMKA VMNELEKSPE
     VILFIDELHT IVGAGGASGS LDASNMFKPA LARGDIQCIG ATTLDEYRQY IEKDGALARR
     FQMVMVDATS IDETIEILNN IKDKYEDHHH VNYTPEAIEA SVKLSERYIS DRFLPDKAID
     VMDEVGARVH ISNITVPEDI LKLEESIENI KKEKNQVVKS QKYEEAAQLR DKEKRLIDQL
     DRAKQAWEED TKKRRYTVTE ENVAEVVAMM TGIPVTSVSN DEGKKLVRMG DELKGKVIGQ
     QSAIDKLVKA IQRTRVGLKD PKKPIGSFIF LGPTGVGKTE LAKVLATYLF DKEDSLVRID
     MSEYMEKFSV SRLVGAPPGY VGYEEGGQLT EKIRRKPYSV VLLDEIEKAH PDVFNILLQV
     LDDGILTDGL GRRVDFRNTI IIMTSNIGVR DLKDFGAGIG FASKRSAESQ DDIMKATIQS
     ALKKAFSPEF LNRLDDVIVF NSLQREDIHH IIDLMLGKLL GRVLNLGYNV ELTEKAKDFL
     AEKGYDPQYG ARPLARAIQR YLEDPVAEEI LKGELKDGDV ILADYSGEGE SLTITVKKPE
     AVTE
//
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