ID S1QYQ8_9ENTE Unreviewed; 338 AA.
AC S1QYQ8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=OMO_00459 {ECO:0000313|EMBL:ESK62209.1};
OS Enterococcus cecorum DSM 20682 = ATCC 43198.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1121864 {ECO:0000313|EMBL:ESK62209.1, ECO:0000313|Proteomes:UP000017415};
RN [1] {ECO:0000313|EMBL:ESK62209.1, ECO:0000313|Proteomes:UP000017415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43198 {ECO:0000313|EMBL:ESK62209.1,
RC ECO:0000313|Proteomes:UP000017415};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus cecorum DSM 20682 (= ATCC 43198)
RT (Illumina assembly).";
RL Submitted (OCT-2013) 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:ESK62209.1}.
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DR EMBL; AHYS01000003; ESK62209.1; -; Genomic_DNA.
DR RefSeq; WP_016252125.1; NZ_KI535313.1.
DR AlphaFoldDB; S1QYQ8; -.
DR STRING; 44008.GCA_001318175_00834; -.
DR GeneID; 60871624; -.
DR PATRIC; fig|1121864.4.peg.1989; -.
DR eggNOG; COG3480; Bacteria.
DR HOGENOM; CLU_042037_2_0_9; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000017415; 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 CDD; cd00987; PDZ_serine_protease; 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 Reference proteome {ECO:0000313|Proteomes:UP000017415};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT ACT_SITE 235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 280
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 338 AA; 38081 MW; 56AADFBD89924771 CRC64;
MKAKRLKKIV SILVFLILLL AFFFYPVNRY VEKPGGIVDL STLVKINNHK DKEKGSFSLT
YVTFQQASCY QLLRSHFEPY WDVLSYEQVL GGSTNQESYD FLQNYYFENA QQMAVYNAFK
AANEKATIQF KGLYVLDFVD GSKAKKQLKV GDIITHVNGQ KLENSLTLFQ FLKNEKPGNQ
LKLTVKRGNK TLTMDITLMK DDQNQAKLGI IIGSDIDLKT SQKVAFDAEG FGGPSAGLMF
TLEIYEQLTK ENIRHGQKIA GTGTMDELGN VGQIGGIDKK IVSADKAGVE LFFVPKDQQK
EDDNEKIAKK VAKQIHTKMK IVPVATFNEA LTYLKNQK
//
