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Database: UniProt
Entry: A0A521EJL8_9SPHI
LinkDB: A0A521EJL8_9SPHI
Original site: A0A521EJL8_9SPHI 
ID   A0A521EJL8_9SPHI        Unreviewed;       845 AA.
AC   A0A521EJL8;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SMO83641.1};
GN   ORFNames=SAMN06265350_11526 {ECO:0000313|EMBL:SMO83641.1};
OS   Solitalea koreensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Solitalea.
OX   NCBI_TaxID=543615 {ECO:0000313|EMBL:SMO83641.1, ECO:0000313|Proteomes:UP000315971};
RN   [1] {ECO:0000313|EMBL:SMO83641.1, ECO:0000313|Proteomes:UP000315971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21342 {ECO:0000313|EMBL:SMO83641.1,
RC   ECO:0000313|Proteomes:UP000315971};
RA   Varghese N., Submissions S.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FXSZ01000015; SMO83641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A521EJL8; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000315971; 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; 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; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SMO83641.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:SMO83641.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:SMO83641.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000315971};
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          437..472
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          148..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          456..483
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        155..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  94773 MW;  27861CA38BD4D1FC CRC64;
     MEAKFSPRVK DVISYSREEA LRLGHDYIGT EHLLLGLIRE GDGIAIKLLK GMAVDTYKLR
     KTIEDAVKGT SGTTVNLGNI PLTKQAEKVL KITYLEAKIF KSEVIGTEHL LLSILRDEDN
     IASQVLNQFN INYEIFKTEL EVNINGIRSE APQSSSDEEN YREEENYGSG KKTGDSKSKT
     PVLDNFGRDL TRAAEDGKLD PIVGREKEIE RVSQILSRRK KNNPILIGEP GVGKSAIAEG
     LALRIVQRKV SRVLFNKRVV TLDLASLVAG TKYRGQFEER MKAVMNELEK SPDVILFIDE
     IHTIVGAGGA SGSLDASNMF KPALARGEIQ CIGATTLDEY RQYIEKDGAL DRRFQKVMVE
     PATIDETKEI LNRIKEKYED HHGVTYTPEA INACVNLTAR YITDRFLPDK AIDALDEAGS
     RVHLTNIHVP ENIIDIEQKI EDIKVEKNRV VRSQKYEEAA KLRDTEKQLL EQLEIAKAEW
     EAETKTKRYI VSEDNVAEVV AMMTGIPVQR VGQADSTKLL NMSDELRTKI IGQDEAIKKL
     TRAIQRTRAG LKDPKKPIGS FIFLGPTGVG KTELAKALSR FMFDTDDSLI QIDMSEYMEK
     FAVSRLVGAP PGYVGYEEGG QLTEKVRRKP YSVILLDEIE KAHPDVYNIL LQVLDEGVLT
     DSLGRKVDFR NTVIIMTSNI GARQLKDFGQ GVGFTTNTKA MNADSHARGV IETALKRAFA
     PEFLNRIDDV IVFNSLSKED IFKIIDIELG QLFGRIHALG YSVQLTDNAK EFIADKGYDP
     SFGARPLNRA IQKYLEDPIA EEILKGEIQE GDIMEVDYDK EKDLITVNLI KESKKRKKKE
     EDNLS
//
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