ID   A0A1H8TRX3_9ACTN        Unreviewed;       421 AA.
AC   A0A1H8TRX3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Protein-L-isoaspartate(D-aspartate) O-methyltransferase/D-alanyl-D-alanine dipeptidase {ECO:0000313|EMBL:SEO93647.1};
GN   ORFNames=SAMN05216267_105731 {ECO:0000313|EMBL:SEO93647.1};
OS   Actinacidiphila rubida.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310780 {ECO:0000313|EMBL:SEO93647.1, ECO:0000313|Proteomes:UP000181951};
RN   [1] {ECO:0000313|EMBL:SEO93647.1, ECO:0000313|Proteomes:UP000181951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2026 {ECO:0000313|EMBL:SEO93647.1,
RC   ECO:0000313|Proteomes:UP000181951};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine; Xref=Rhea:RHEA:20661,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822;
CC         EC=3.4.13.22; Evidence={ECO:0000256|ARBA:ARBA00001362};
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DR   EMBL; FODD01000057; SEO93647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8TRX3; -.
DR   STRING; 310780.SAMN05216267_105731; -.
DR   Proteomes; UP000181951; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000755; A_A_dipeptidase.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43126; D-ALANYL-D-ALANINE DIPEPTIDASE; 1.
DR   PANTHER; PTHR43126:SF2; D-ALANYL-D-ALANINE DIPEPTIDASE; 1.
DR   Pfam; PF13671; AAA_33; 1.
DR   Pfam; PF01427; Peptidase_M15; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Methyltransferase {ECO:0000313|EMBL:SEO93647.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000181951};
KW   Transferase {ECO:0000313|EMBL:SEO93647.1}.
FT   REGION          186..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  46466 MW;  B3BC66AAEE8EBCA3 CRC64;
     MAHMTAPPHR VSTGTAVGRE DTRLVVIRGN SASGKSSVAQ GLRDHYGRGV AIVGQDVIRR
     NVLREHDTTG GANIALLARI ARHALDAGFH VVLEGILYAD RYSHMITTLV RDHRGVSRCY
     YLDVPLEATL VRHASKADAT YLTQVTDDHL ASWYRELDLL PGSLETEIPA DSTLQDTIAR
     IVRETGLAHA SPTPPPQRKP SQGDSMNPLV LMSDPQVAAI PVRECGEPLV DVRHHDFRVD
     LRKQDPLGAF AHVREGVLAR LQQARSLLPA GTDLLFIEGY RPLSLQQRYF TEYRDELAAT
     HPDWTADELH QAASRYVSPP EIAPHSAGAA VDVTLVDQDG HELDLGTRVN ATPEESDGAC
     YTHAPNLSDQ ARHHRTLLLN AMQAAGFTNY GTEFWHFSAA DRYDALMRQE PHARYGPIEL
     P
//