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Database: UniProt
Entry: A0A142L5I0_9BACT
LinkDB: A0A142L5I0_9BACT
Original site: A0A142L5I0_9BACT 
ID   A0A142L5I0_9BACT        Unreviewed;       848 AA.
AC   A0A142L5I0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:AMS27476.1};
GN   ORFNames=AEM51_11040 {ECO:0000313|EMBL:AMS27476.1};
OS   Bacteroidetes bacterium UKL13-3.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1690483 {ECO:0000313|EMBL:AMS27476.1, ECO:0000313|Proteomes:UP000075224};
RN   [1] {ECO:0000313|Proteomes:UP000075224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Driscoll C.B.;
RL   Submitted (JUL-2015) 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; CP012155; AMS27476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142L5I0; -.
DR   STRING; 1690483.AEM51_11040; -.
DR   KEGG; bbau:AEM51_11040; -.
DR   PATRIC; fig|1690483.4.peg.2350; -.
DR   Proteomes; UP000075224; 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:AMS27476.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AMS27476.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075224};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          436..471
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          149..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          455..489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        150..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   848 AA;  95467 MW;  0B3FC720F3E12783 CRC64;
     MEAKFSPRVK DVISYSREEA IRLGHDYIGT EHLLLGLIRE GDGKAIKTIK ALDIDSIRLK
     KTIEDAIKGT ATNNTNLVNI PLTKQAEKVL KITYLEAKIF KTDIIGTEHL LLSILRDEDN
     LASQILSQYG VSYDIFKAAI ENNISDVRSE MPQDSEEEYY REERKPQEPV RKGEVKSKTP
     VLDNFGRDLT KSAEDGKLDP IVGREKEIER VSQILSRRKK NNPVLIGEPG VGKTAIAEGL
     ALRIVQRKVS RVLFNKRVIM LDLASLVAGT KYRGQFEERM KAVMNELEKS PDVILFIDEI
     HTIVGAGGAS GSLDASNMFK PALARGEIQC IGATTLDEYR QYIEKDGALE RRFQVVMVNP
     ASPEETVEIL HNIKSKYEDH HSVTYEDTAI DACVAMSNRY MTDRHLPDKA IDVLDEVGAR
     VHISNIHVPQ NVLNLEKMIE DIKVEKNKVV KSQKYEEAAK LRDREKHLLE QLETEKAKWE
     EETKSQRYKV TEDDVADVIA MMTGIPVKRI AQSEGLRLLN MGTELQGRVI GQDDAIKKLA
     KAIQRNRAGL KNPNKPIGSF VFLGPTGVGK TEMAKVLARY LFDSDDAMIR IDMSEYMEKF
     AVSRLVGAPP GYIGYEEGGQ LTEKIRRKPY AVLLLDEIEK AHPDVFNILL QVLDEGFLTD
     SLGRKVDFRN TIIIMTSNIG SRQLKDFGQG VGFGTPSKNA QQDTHAKVVI ENALKRFFSP
     EFLNRIDDVI VFNSLDKEAI TKILDLNMEK LVKRVEELAY TFKITDEAKT FLAEKGFDPD
     MGARPLARTI QRFVEDPIAE ELLKGEAGEG SVIEVDYMKD EPELKITVSK KKEPRKKKDA
     PPVNPTDN
//
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