ID A0A099WG68_9LIST Unreviewed; 348 AA.
AC A0A099WG68;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=EP56_04085 {ECO:0000313|EMBL:KGL44739.1};
OS Listeriaceae bacterium FSL A5-0209.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae.
OX NCBI_TaxID=1497679 {ECO:0000313|EMBL:KGL44739.1, ECO:0000313|Proteomes:UP000029855};
RN [1] {ECO:0000313|EMBL:KGL44739.1, ECO:0000313|Proteomes:UP000029855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0209 {ECO:0000313|EMBL:KGL44739.1,
RC ECO:0000313|Proteomes:UP000029855};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing plants.";
RL Submitted (MAY-2014) 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:KGL44739.1}.
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DR EMBL; JNEZ01000011; KGL44739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099WG68; -.
DR STRING; 1497679.EP56_04085; -.
DR eggNOG; COG3480; Bacteria.
DR Proteomes; UP000029855; 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; 2.30.42.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; NF041438; SepM_fam_S16; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF48; ENDOPEPTIDASE LA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 101..162
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 226..345
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 348 AA; 38109 MW; 6314424276CDF8FA CRC64;
MKKNWKKFLA GLIVLALVVA FFVPLPYYVT RPGSADKLSP LVTVEGHPSN SEGVFRLVTI
AMGQANIYSY LAAKMLPYQE IEKESDVRGE NETDEEYNVR QLSLMNQSKN NAIQVAYKAA
GQSVKIEYRG VYVLSVMPDA PAAKVLEAGD LITAIDGKSF ESSAEFIDYV RSKKVGDKVE
VSYKHQDKSE KASVELIDID KKGTPGIGIS LVDDQKLVTD PKITIDSEKI GGPSAGLMFT
LEIYNHFGKT DWTKGHNIAG TGTIDVDGNV GRIGGIDQKI VAADRDDVEI FFAPDDTITP
EMKKAQPGVA SNYEDAVKTA KAIDSKMKVV PVKTFQDALD YLKTLKEK
//
