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Database: UniProt
Entry: A0A1M3BJZ7_9ACTN
LinkDB: A0A1M3BJZ7_9ACTN
Original site: A0A1M3BJZ7_9ACTN 
ID   A0A1M3BJZ7_9ACTN        Unreviewed;       282 AA.
AC   A0A1M3BJZ7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   RecName: Full=Peptidase E {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO11_13205 {ECO:0000313|EMBL:OJU84529.1};
OS   Solirubrobacterales bacterium 70-9.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX   NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU84529.1, ECO:0000313|Proteomes:UP000184118};
RN   [1] {ECO:0000313|EMBL:OJU84529.1, ECO:0000313|Proteomes:UP000184118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-9 {ECO:0000313|EMBL:OJU84529.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJU84529.1}.
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DR   EMBL; MKSH01000075; OJU84529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3BJZ7; -.
DR   Proteomes; UP000184118; 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; 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; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR   PANTHER; PTHR20842:SF0; SI:DKEY-69O16.5; 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:ARBA00022825};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ   SEQUENCE   282 AA;  30084 MW;  8B655BF2E2691D46 CRC64;
     MPGLDAGIGE NGATPGETTP VRRILTLGGH EFSSRPPDRA VCEFLLRLAT ERGGTRPRIC
     ILPTASGDTS DLISSFYSAF NDRPCEPSDV SLFRLGRRPM ALRDHLLSQD LIYVGGGSMV
     NLLAVWEAHG IASILALAWQ RGIVLAGQSA GAMCWFEAGI TTSSGKPLEA AGLGLLHGSL
     CVHYNNEPAR RAAYLEAVGK GMPAGYGLDD YAGLLWEGED SPAAVTARRG ARAYRVSARD
     GVASESPLPA RFLPAPAPAA LREDIAEFRR IKTMRRRAGW LG
//
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