ID A0A3B8L0Z4_9BACT Unreviewed; 840 AA. AC A0A3B8L0Z4; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 28-JUN-2023, entry version 16. DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122}; DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122}; DE Flags: Fragment; GN ORFNames=DCE03_05900 {ECO:0000313|EMBL:HAA48000.1}; OS Synergistaceae bacterium. OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae. OX NCBI_TaxID=2053624 {ECO:0000313|EMBL:HAA48000.1, ECO:0000313|Proteomes:UP000261061}; RN [1] {ECO:0000313|EMBL:HAA48000.1, ECO:0000313|Proteomes:UP000261061} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA9913 {ECO:0000313|EMBL:HAA48000.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01122}; CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE- CC ProRule:PRU01122}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HAA48000.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DLVO01000135; HAA48000.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3B8L0Z4; -. DR Proteomes; UP000261061; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR041699; AAA_32. DR InterPro; IPR046844; Lon-like_helical. DR InterPro; IPR008269; Lon_proteolytic. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR046843; LonB_AAA-LID. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1. DR PANTHER; PTHR10046:SF46; ENDOPEPTIDASE LA; 1. DR Pfam; PF13654; AAA_32; 1. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF20436; LonB_AAA-LID; 1. DR Pfam; PF20437; LonC_helical; 1. DR PRINTS; PR00830; ENDOLAPTASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU01122}; Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}. FT DOMAIN 588..783 FT /note="Lon proteolytic" FT /evidence="ECO:0000259|PROSITE:PS51786" FT REGION 186..226 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 820..840 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 186..203 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 678 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122" FT ACT_SITE 721 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122" FT NON_TER 840 FT /evidence="ECO:0000313|EMBL:HAA48000.1" SQ SEQUENCE 840 AA; 94044 MW; 4D2DE1C63381BFF4 CRC64; MKKASLPLKI EDLRKRTNPD SLGLETTRDV ECLDALIGQE RAVKSISFGL EVQNKGYNIF VVGDHGSGRT TYSLERIRDR ARSEKTPDDV IYVYNFKNPD EPLAINIPAG QGEKLASHLD DLVEELKSAL SKAFENSQYE DAKAQLVKEF QEQVNTLMEE LRTWAAEKGF AIKRTPQGFV NIPLVEEEKS EADQQKNGID SDEKDAGNSG NGPGKKLKEM QQEDFEALSE EEKKALQEAS EEVSQKTLEV LRKIRDKEKT LKEKIRDLEA EICRSAIRPY LQETKERFQA EGKLGEWIDA LTEDIIENFN IFVAAARDDS GPEVDFSRYS VNVFVSNDPE AGAPVIWETN PTYYNLCGKI EYESRQGVLT TDFRKVVAGA IQRANGGYLV LHAEEVLRNF MSWDALKRAL RTQELAVENL GEQLGMIPVS SLRPQPVQLR TKVVLIGTPW LYYLLNIYDP EVQKLFKIKA DFDVDMPRTA ETQKQMACFV SGYVTKEGHR HFSAEGIAEL IEWSSRLAGH SERMSTQFNK ITEVIVEASA WAGTEGEVTV GSRHVRKALK EKAFRVNLVE ERLHRAFSEK TIRIQTHGER IGQINGLTVV DMRDHVFGHP VRITANVYMG SEGIVNIERE VKMTGPIHNK GLLILGSYLG KKYAQDMPLS LTARITFEQT YSGVEGDSAS STELYCLLSA LSDVPLRQGI AVTGSVDQHG NIQPIGGVNE KIEGFFEYCK TSGLTGNQGV IIPKQNVKNL MLDHELITAV EEGKFNIWPV ETIEEGIEIL TGIPAGEPDE KGGYPEGTIH GKAMKKLRGW VKKAARLKKE VETMEESAVR PDEDPDEGDS //