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Database: UniProt
Entry: A0A1A9I760_9BACT
LinkDB: A0A1A9I760_9BACT
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ID   A0A1A9I760_9BACT        Unreviewed;       843 AA.
AC   A0A1A9I760;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:ANH82540.1};
GN   ORFNames=A8C56_17560 {ECO:0000313|EMBL:ANH82540.1};
OS   Niabella ginsenosidivorans.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=1176587 {ECO:0000313|EMBL:ANH82540.1, ECO:0000313|Proteomes:UP000077667};
RN   [1] {ECO:0000313|EMBL:ANH82540.1, ECO:0000313|Proteomes:UP000077667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS26 {ECO:0000313|EMBL:ANH82540.1,
RC   ECO:0000313|Proteomes:UP000077667};
RA   Im W.T., Siddiqi M.Z.;
RT   "Niabella ginsenosidivorans BS26 whole genome sequencing.";
RL   Submitted (MAY-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; CP015772; ANH82540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9I760; -.
DR   STRING; 1176587.A8C56_17560; -.
DR   KEGG; nia:A8C56_17560; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000077667; 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:ANH82540.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ANH82540.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077667};
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          148..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..487
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   843 AA;  95196 MW;  D9255BF63F1F1FBA CRC64;
     MDNNFSSQVK EIISYSREEA LRLGNDFIGT EHLLLGLIRE GDNTAIRILK SFSVDIFELR
     KEIELAIKDK TGKNIANINS LPLTKQAEKV IRVTVLEAKA LKSNQVETEH LMLSILKNKE
     NIATQILNQF DVDYDLFRQE LGIVKSGGEP RAEFGEEGEE EFEEEKKYSQ SRSSTSKTAT
     KSKTPVLDNF GRDVTKLAES GNLDPIVGRE KEIERVSQIL SRRKKNNPIL IGEPGVGKTA
     IVEGLALRIV QRKVSRVLFD KRVISLDLAS LVAGTKYRGQ FEERMKAIMN ELEKNRDVIL
     FIDEMHTIVG AGGASGSLDA SNIFKPALAR GELQCIGAST LDEYRMYIEK DGALDRRFQK
     VMVDPPSVEE TIQILNNIKS KYEDFHSVTY SPEAIEACVK LSDRYITDRL LPDKAIDVMD
     EVGARVHLKN INVPQNIVDL EKKIEDIKEE KNKVVKSQKF EEAASLRDTE KKLAEDLEQA
     KAAWEEESKH KRYPIDEEAI AEVINIMTGI PVRKMVEAET EKLRKMSDDM RNMVIGQNEA
     ISKVVKAIQR NRVGLKDPKK PIGTFIFLGP TGVGKTELAR SLARYLFDSE DALIRIDMSE
     YMEKFTVSRL IGAPPGYVGY EEGGQLTEKV RRKPYSVILL DEIEKAHPDI YNILLQVLDD
     GVLTDGLGRK VDFKNTIIIM TSNIGVRQLK DFGAGVGFAT SARIENEDEE NKAVIEKALK
     RTFSPEFLNR IDDVIIFNSL TRENIFSIID ISMKGVLKRV TNLGYGLELS EEAKTFLADK
     GYDQQFGARP LHRAIQKYLE DPLAEEILNM HVKPGDVLLV EFDKEKDKLY FTVKNPKENP
     QEA
//
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