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Database: UniProt
Entry: R7ETS1_9FIRM
LinkDB: R7ETS1_9FIRM
Original site: R7ETS1_9FIRM 
ID   R7ETS1_9FIRM            Unreviewed;       288 AA.
AC   R7ETS1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Peptidase S51 dipeptidase E {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN640_01739 {ECO:0000313|EMBL:CDE05648.1};
OS   Anaerotruncus sp. CAG:390.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=1262703 {ECO:0000313|EMBL:CDE05648.1, ECO:0000313|Proteomes:UP000018385};
RN   [1] {ECO:0000313|EMBL:CDE05648.1, ECO:0000313|Proteomes:UP000018385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:390 {ECO:0000313|Proteomes:UP000018385};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDE05648.1}.
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DR   EMBL; CBID010000291; CDE05648.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7ETS1; -.
DR   STRING; 1262703.BN640_01739; -.
DR   Proteomes; UP000018385; 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   CDD; cd03129; GAT1_Peptidase_E_like; 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   Reference proteome {ECO:0000313|Proteomes:UP000018385};
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..288
FT                   /note="Peptidase S51 dipeptidase E"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039395103"
FT   REGION          30..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   288 AA;  31561 MW;  A11596BFA898688D CRC64;
     MNNSIRLAAV LAGLAVCICL CLAACRKETP GGENTATDTA GVGSDMSDTP GESTDPPVPV
     VKKAVIAGGG ASTKIYSEIV GLADKKDPKV IILCTAGKDT VSNVEAYVNT FKRLTKNVEA
     ITLVTKLYDP QELHDKIVNA DIICVGGGQS EYMDMVWKKF KVNEYLVEAY NKGVICCGGS
     AGGMCWTYMG WNDYYSVPDS IYKFFPGLDV VNIYYGPHFD SSDKWAEFDR AIMKETSPKY
     DLGFAMDNGT AIVFIDGVPT RSVREKETSR IIRYDFRDGK WTRSVYTD
//
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