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Database: UniProt
Entry: A0A1T5BD69_9SPHI
LinkDB: A0A1T5BD69_9SPHI
Original site: A0A1T5BD69_9SPHI 
ID   A0A1T5BD69_9SPHI        Unreviewed;       850 AA.
AC   A0A1T5BD69;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SKB45168.1};
GN   ORFNames=SAMN05660226_01395 {ECO:0000313|EMBL:SKB45168.1};
OS   Parapedobacter luteus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Parapedobacter.
OX   NCBI_TaxID=623280 {ECO:0000313|EMBL:SKB45168.1, ECO:0000313|Proteomes:UP000190541};
RN   [1] {ECO:0000313|EMBL:SKB45168.1, ECO:0000313|Proteomes:UP000190541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22899 {ECO:0000313|EMBL:SKB45168.1,
RC   ECO:0000313|Proteomes:UP000190541};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FUYS01000003; SKB45168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5BD69; -.
DR   STRING; 623280.SAMN05660226_01395; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000190541; 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:SF193; CHAPERONE PROTEIN CLPB; 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:SKB45168.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:SKB45168.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:SKB45168.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190541};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
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          147..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          456..483
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        156..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  95348 MW;  35CDFE55B6FB62AC CRC64;
     MEAKFSPRVK DVISYSREEA IRLKHDYIGT EHLLLGLIRE GDGMAIKILK HAGIDTTELR
     KSIEDAVKGS SMSRAPIGNM PLTKQAEKVL KITYLEAKIF KSDIIGTEHL LLSILRDEDN
     IASQILQQYD INYDVFKADV EQHKAGITDQ ASGSTAGDDD FKDEDHFSQP KKVSDIKSKT
     PVLDNFGRDL TRAAEEGRLD PIVGREKEIE RVSQILSRRK KNNPILIGEP GVGKSAIAEG
     LALRIIQRKV SRVLFNKRVV TLDLASLVAG TKYRGQFEER MKAVMNELEK SPDVILFIDE
     IHTIVGAGGA SGSLDASNMF KPALARGEIQ CIGATTLDEY RQYIEKDGAL DRRFQKVMIE
     PATHDETVEI LNRIKEKYEE HHNVNYTPEA IEACVTLTTR YITDRFLPDK AIDALDEAGS
     RVHLTNIHVP QSIIDIEQKI EEIKVEKNKV VRSQKYEEAA KLRDTEKKLL EELEHEKAAW
     EAETKTKRYT VTEDNVAEVV SMMTGIPVQR VGQSDSQKLL NMAESMKGRI IGQDEAVKKL
     VKAIQRTRAG LKDPKKPIGS FIFLGPTGVG KTELAKELAR FMFDSEDSLI QIDMSEYMEK
     FAISRLVGAP PGYVGYEEGG QLTEKVRRKP YAVVLLDEIE KAHPDVFNLL LQVLDEGQLT
     DSLGRRVDFR NTILIMTSNI GARQLKDFGQ GVGFTTSAKA EQAESHSRSV IENALKRAFA
     PEFLNRIDDV IVFNSLDKEH IFKIIDIELK SLFVRIEALG YRIKLTDGAK EFIAEKGFDS
     NFGARPLKRA IQKYLEDPIA EEILKGVVAE GNTLEVDYDK DKQEIVVNVQ AADSGSSRPS
     DFAEEKKEDE
//
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