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Database: UniProt
Entry: U7SS12_FUSNU
LinkDB: U7SS12_FUSNU
Original site: U7SS12_FUSNU 
ID   U7SS12_FUSNU            Unreviewed;       238 AA.
AC   U7SS12;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Dipeptidase E {ECO:0000313|EMBL:ERT35028.1};
GN   ORFNames=HMPREF1766_01503 {ECO:0000313|EMBL:ERT35028.1};
OS   Fusobacterium nucleatum CTI-5.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=1316586 {ECO:0000313|EMBL:ERT35028.1, ECO:0000313|Proteomes:UP000017135};
RN   [1] {ECO:0000313|EMBL:ERT35028.1, ECO:0000313|Proteomes:UP000017135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTI-5 {ECO:0000313|EMBL:ERT35028.1,
RC   ECO:0000313|Proteomes:UP000017135};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Kostic A., Garrett W.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S.,
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., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium nucleatum CTI-5.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S51 family.
CC       {ECO:0000256|ARBA:ARBA00006534}.
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:ERT35028.1}.
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DR   EMBL; AXNW01000020; ERT35028.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7SS12; -.
DR   PATRIC; fig|1316586.3.peg.1468; -.
DR   HOGENOM; CLU_090997_0_0_0; -.
DR   Proteomes; UP000017135; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..238
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004687873"
SQ   SEQUENCE   238 AA;  27478 MW;  A0FB866272CA75B3 CRC64;
     MKKSVLKIFC LLTFIFISQF SFSNNFNNNK GDGRKMKKLF LCSYFAGVKD TFKDFMNNDT
     KGKKVLFIPT ANIDEESKFL VDEAKEVFKN LGMEVEDLEI SKLDEKTIKN KIEKTNYLYV
     GGGNTFYLLQ ELKRKNLIDF IKNRVNSGMV YIGESAGAII TSKDIEYNDS MDDKTIAKDL
     KEYSGLNLVD FYIVPHLNEF PFEESSKQTV EKYKDKLNII AINNSQAIIV KDEKYEIK
//
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