ID A0A1L8TCQ7_9ENTE Unreviewed; 347 AA.
AC A0A1L8TCQ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN ORFNames=RV04_GL001157 {ECO:0000313|EMBL:OJG41998.1};
OS Enterococcus hermanniensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=249189 {ECO:0000313|EMBL:OJG41998.1, ECO:0000313|Proteomes:UP000182077};
RN [1] {ECO:0000313|EMBL:OJG41998.1, ECO:0000313|Proteomes:UP000182077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17122 {ECO:0000313|EMBL:OJG41998.1,
RC ECO:0000313|Proteomes:UP000182077};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-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:OJG41998.1}.
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DR EMBL; JXKQ01000020; OJG41998.1; -; Genomic_DNA.
DR RefSeq; WP_071858779.1; NZ_JXKQ01000020.1.
DR AlphaFoldDB; A0A1L8TCQ7; -.
DR STRING; 249189.RV04_GL001157; -.
DR OrthoDB; 2356897at2; -.
DR Proteomes; UP000182077; 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 SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000182077};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 227..346
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 280
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 347 AA; 38201 MW; 46C2AFBE44F29CF4 CRC64;
MKKNKLVKRL LLIFVALVAV ACVVVPLPYY IEEPGDTINL KELITVNDQK DDQKGSFSLT
SVGIRRATVF TMAKAKFEPF YEIISAEDLT GGASDEEYLQ IQQFYMETSQ NFAIEQAMKL
ANKPYEMKYK GVYVLGVEKN SNFAGKISIG DTITKADGKE FTSSDEFMKY VKSQKVGQEM
KVTYIHDGKT KEATEKLIKL PTDKKPGIGI SLTDHTEIES QEKVKINAGS IGGPSAGLMF
TLEVYQQLVD KDLRHGQKIA GTGTMDSEGN VGRIGGIDKK VASASASGAK IFFAPNDEIT
KEMKKAQPGI KSNYEEAKAA VKKLDTDMKI VPVKTAQDAI DYLAQMK
//
