ID   A0A2C9XFN1_9ENTE        Unreviewed;       416 AA.
AC   A0A2C9XFN1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptidase C51 domain-containing protein {ECO:0000259|PROSITE:PS50911};
GN   ORFNames=A5880_003172 {ECO:0000313|EMBL:OTO02776.1};
OS   Enterococcus sp. 4G2_DIV0659.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1834181 {ECO:0000313|EMBL:OTO02776.1, ECO:0000313|Proteomes:UP000195139};
RN   [1] {ECO:0000313|EMBL:OTO02776.1, ECO:0000313|Proteomes:UP000195139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G2_DIV0659 {ECO:0000313|EMBL:OTO02776.1,
RC   ECO:0000313|Proteomes:UP000195139};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA   Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sp. 4G2_DIV0659.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC       {ECO:0000256|ARBA:ARBA00010266}.
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:OTO02776.1}.
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DR   EMBL; NGLE01000006; OTO02776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9XFN1; -.
DR   STRING; 1834181.A5880_003172; -.
DR   OrthoDB; 9805070at2; -.
DR   Proteomes; UP000195139; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   InterPro; IPR007921; CHAP_dom.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF05257; CHAP; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50911; CHAP; 1.
PE   3: Inferred from homology;
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          277..412
FT                   /note="Peptidase C51"
FT                   /evidence="ECO:0000259|PROSITE:PS50911"
FT   REGION          232..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  44578 MW;  1BB9E2EEF3E94112 CRC64;
     MKKAKWGCML FPIILLLGVL FFLIVLVGGE PKSESGCIQS NWDNPDDGKT VPASIEEFVK
     SHREAYILSW KAGGFLPSAS IAQTMVENGF NFTNPSGTSF WQAHNMGGVK TSRKEDFPIT
     LGVFGEDSVD ITGTKPGTNV GDNTGGAYTW FKDYNAGIVG KAEFMAHQTL YTRAINNTDG
     VSALTAIFEG GWATDPSYLM KLLATYSSLG TQFQWLDKEA ILKYGSTPYQ GKNDLDEGTV
     NVPKGEESDS SDCVKTSDTA GQVTGENSAP TLEVPKEYQG KLTLPPPDSK DYSGNSYPFG
     ECTWGAYNRM AQIGNRIEWF SGDSGHGGAW GASARSAGYT VVKGEPKVGW AACFQGGVAG
     SLPPYGHIAV VEYVNSDGSI LVSETNVINM GSGTRSWRVL DKGIVSQLEF IQGKGG
//