GenomeNet

Database: UniProt
Entry: A0A2A2YAT6_9BACT
LinkDB: A0A2A2YAT6_9BACT
Original site: A0A2A2YAT6_9BACT 
ID   A0A2A2YAT6_9BACT        Unreviewed;       229 AA.
AC   A0A2A2YAT6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=CAK88_07040 {ECO:0000313|EMBL:PAZ05826.1};
OS   Verrucomicrobiae bacterium AMD-G2.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX   NCBI_TaxID=1982328 {ECO:0000313|EMBL:PAZ05826.1, ECO:0000313|Proteomes:UP000217571};
RN   [1] {ECO:0000313|EMBL:PAZ05826.1, ECO:0000313|Proteomes:UP000217571}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMD-G2 {ECO:0000313|EMBL:PAZ05826.1};
RA   Cabello-Yeves P.J., Ghai R., Mehrshad M., Picazo A., Camacho A.,
RA   Rodriguez-Valera F.;
RT   "Genome diversity of Verrucomicrobia from freshwater lakes.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001561};
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:PAZ05826.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NEUM01000013; PAZ05826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2YAT6; -.
DR   Proteomes; UP000217571; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF11; N-ACETYLMURAMOYL-L-ALANINE AMIDASE XLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   4: Predicted;
KW   Competence {ECO:0000256|ARBA:ARBA00023287};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT   DOMAIN          59..211
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   229 AA;  25685 MW;  2EA69A0C4AE394D4 CRC64;
     MIIGVCCTPV APIGGRADRP IEWAARSGSA PVSAGSVGSL NSIMRGVNLR QDLVPRGSHG
     RKVFRSMSPR YITIHSTQNW SADAWKHSQA LKNGALRAPK RRGGNRIGYL IWHFTVDDKV
     ALQHMPTNEQ GEHADFDGPG NRYSIGIEMC EQRGSNLNTT MDRTARLAAY LMIKNGIPLR
     NVVPHYHWPR RGASPPHKNC PHFLMTNGRP GSKWRVFLGK VDYYYRQMK
//
DBGET integrated database retrieval system