ID E5WEK5_9BACI Unreviewed; 214 AA.
AC E5WEK5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Peptidase S51 dipeptidase E {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1013_00880 {ECO:0000313|EMBL:EFV78996.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV78996.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV78996.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV78996.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-2010) 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:EFV78996.1}.
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DR EMBL; ACWD01000011; EFV78996.1; -; Genomic_DNA.
DR RefSeq; WP_009331382.1; NZ_GL635750.1.
DR AlphaFoldDB; E5WEK5; -.
DR eggNOG; COG4242; Bacteria.
DR HOGENOM; CLU_104556_0_0_9; -.
DR Proteomes; UP000003283; 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; PTHR36175; CYANOPHYCINASE; 1.
DR PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 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:UP000003283};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 214 AA; 23486 MW; 54F48C5671B84857 CRC64;
MDSRHLFLMG GSPPFGQRLG KKFTELACGA AGKIAILFLE REGWEGYMNK YTSGLTQNGA
RNFCYLPLSP APPESFLQEL VSCTGIIIGG GETEKYRSYI VDTEVGEYIG KMYKNGIPVA
GFSAGALIIP EHCIIPPIDT SEKQHLFLKG IGLIRDCVIS VHFTKWNEGE NLKRAAGKTN
VTAGYGIDDD AGIYFYNEIQ TDSEGGIHIY MNEI
//
