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
//