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Database: UniProt
Entry: L0ISI0_9MYCO
LinkDB: L0ISI0_9MYCO
Original site: L0ISI0_9MYCO 
ID   L0ISI0_9MYCO            Unreviewed;       237 AA.
AC   L0ISI0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Peptidase E {ECO:0000313|EMBL:AGB20932.1};
GN   ORFNames=Mycsm_00481 {ECO:0000313|EMBL:AGB20932.1};
OS   Mycobacterium sp. JS623.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB20932.1, ECO:0000313|Proteomes:UP000010844};
RN   [1] {ECO:0000313|Proteomes:UP000010844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA   Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S51 family.
CC       {ECO:0000256|ARBA:ARBA00006534}.
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DR   EMBL; CP003078; AGB20932.1; -; Genomic_DNA.
DR   RefSeq; WP_015304523.1; NC_019966.1.
DR   AlphaFoldDB; L0ISI0; -.
DR   STRING; 212767.Mycsm_00481; -.
DR   KEGG; msa:Mycsm_00481; -.
DR   PATRIC; fig|710686.3.peg.480; -.
DR   HOGENOM; CLU_067063_1_0_11; -.
DR   OrthoDB; 9778515at2; -.
DR   Proteomes; UP000010844; Chromosome.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03146; GAT1_Peptidase_E; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005320; Peptidase_S51.
DR   PANTHER; PTHR20842:SF0; ALPHA-ASPARTYL DIPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR   Pfam; PF03575; Peptidase_S51; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ   SEQUENCE   237 AA;  25584 MW;  73FC6E4A0036B97A CRC64;
     MPADAPTILA TSGGFREGQR TRWEFSELTE YAIELAGVSG RAPRLCFVAT AVGDNPTVLH
     WLIDAAQARG FHASHLTLFP MPNVDDITAH LLDHDVVWVF GGSVAGLLAM WRLHGVDTAM
     RTAWQAGVVL TGISAGSICW HVGGTTDSFG PELRPVTDGL GLVPYSNGVH YDSEPQRRPL
     FQRLIADGAL PAGYATDDGA GILYRGTDFV EAVSERDCAA AYFVDDAKES RLETRRL
//
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