ID A0A1S2KCT5_9ACTN Unreviewed; 407 AA.
AC A0A1S2KCT5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:OII65950.1};
GN ORFNames=BJP40_15120 {ECO:0000313|EMBL:OII65950.1};
OS Streptomyces sp. CC53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII65950.1, ECO:0000313|Proteomes:UP000179639};
RN [1] {ECO:0000313|EMBL:OII65950.1, ECO:0000313|Proteomes:UP000179639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC53 {ECO:0000313|EMBL:OII65950.1,
RC ECO:0000313|Proteomes:UP000179639};
RA Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT transport.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OII65950.1}.
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DR EMBL; MKXB01000020; OII65950.1; -; Genomic_DNA.
DR RefSeq; WP_071278047.1; NZ_MKXB01000020.1.
DR AlphaFoldDB; A0A1S2KCT5; -.
DR STRING; 1906740.BJP40_15120; -.
DR Proteomes; UP000179639; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd08014; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:OII65950.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179639}.
FT DOMAIN 203..295
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 43422 MW; E7A7AAF3D4DA76C2 CRC64;
MSREPEADVP GETPLPGTLP EPLRAELIAF RRDLHMHPEL GNQEFRTTAA IKSRLEAAGL
RPRVLPGGTG LTCDIGTWDG HRPMLAIRAD IDALPIPDTK ADCPYRSTVP DRAHACGHDV
HTTTVLGTGL VLAELHRKGL LARPVRLVFQ PAEEVLPGGA VNAVEAGVLD GVGKIIAVHC
DPRVDAGKIG LRVGPITSAC DRLEVTLDGP GGHTARPHLT TDLVTAVARV ATDVPALLAR
RIDARSGLVL TWGRIEAGHA PNVIPQHAEL GGTVRCLDLA AWRDAPDQVY AAIDEVATLH
GAKSTINYVR GVPPVVNDPV IAELLREAMT RRCGPYAIED TEQSLGGEDF SWYLEHVPGA
MARLGVRRPG DPNHLDLHRG NFDVDESAIK VGVEMFTAAA LIDAGTV
//
