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Database: UniProt
Entry: A0A1V2M9P7_9FIRM
LinkDB: A0A1V2M9P7_9FIRM
Original site: A0A1V2M9P7_9FIRM 
ID   A0A1V2M9P7_9FIRM        Unreviewed;       751 AA.
AC   A0A1V2M9P7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   ORFNames=AN641_00995 {ECO:0000313|EMBL:ONI45028.1};
OS   Epulopiscium sp. SCG-C07WGA-EpuloA2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Candidatus Epulonipiscium.
OX   NCBI_TaxID=1712378 {ECO:0000313|EMBL:ONI45028.1, ECO:0000313|Proteomes:UP000189533};
RN   [1] {ECO:0000313|Proteomes:UP000189533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ngugi D.K., Miyake S., Stingl U.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:ONI45028.1}.
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DR   EMBL; LJHE01000045; ONI45028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2M9P7; -.
DR   Proteomes; UP000189533; 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; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046:SF46; ARCHAEAL LON PROTEASE; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF20437; LonC_helical; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000189533};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          537..732
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          129..161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        627
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        670
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   751 AA;  85478 MW;  B822951F5D78E2FE CRC64;
     MVKELCWTQL KDLFQPSDFY FETIEQISGS DTFLGQDEAI NALNFALNLN NYNIFIASEE
     SFLDEIIKII EEKALFLNVP EDLCYVYNFE EPNKPKILYL EAGDGKILQD DLKEFVIFLK
     NELSERLKSL KLEDKKQELI KDFEEQKNEI LEKLNQEVKE LGFNISQVEG GLAFSIIDEN
     NIINLEENSN KIKQLARIAL DQINIWEQEI GAILNNLYEE ELIRQISGPI HILKIKYKYY
     TEFIDYFDNI FEDILEHSDL FIENEDENTE VLKGIFPIMN KSNLSEFLKR YEVNLIVNNS
     NKKGAPVIVA QDSDYRSLMG SITLKDTVDI SSIKAGALQQ ARGGFLILKA EDIIERLGGW
     QAIKQTLNSG FIKMEDLKND SINVPQILEP EKIKANVRII LVGSSVHYDL LKNYEPSFSK
     LFKFRIDFLD EANYTKEIIE QIGYVINKQC KKEKLKPVTT QALLNAIRKT QYRIDKISLN
     VEPIYKLIYQ ANSIAKDKIT EVDIENVDKF NKTLLNKINN DMKENYKLNR TLIDVDGSKI
     GEINGLCIYD IGENTIGHPI KITATSYKGK KGIINIEKAA GISGSIHSKG VEIIEGFLGG
     RFAKTIEPSL NCKICIEQNY ASIDGDSASS AELYAVISSL CGIPLKQNLA VTGSINQYGD
     IQPVGGLSEK IEGFFKACQQ KGLTNDQGVI IPYQNQVDLI LTNEIIEHIQ EGKFHIYPIK
     RYEQGIELLT GESARRVEEK VRQVLKLMVI K
//
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