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Database: UniProt
Entry: A0A239KLM5_9FIRM
LinkDB: A0A239KLM5_9FIRM
Original site: A0A239KLM5_9FIRM 
ID   A0A239KLM5_9FIRM        Unreviewed;       217 AA.
AC   A0A239KLM5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SAMN05446037_10498 {ECO:0000313|EMBL:SNT18499.1};
OS   Anaerovirgula multivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Anaerovirgula.
OX   NCBI_TaxID=312168 {ECO:0000313|EMBL:SNT18499.1, ECO:0000313|Proteomes:UP000198304};
RN   [1] {ECO:0000313|EMBL:SNT18499.1, ECO:0000313|Proteomes:UP000198304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCA {ECO:0000313|EMBL:SNT18499.1,
RC   ECO:0000313|Proteomes:UP000198304};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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DR   EMBL; FZOJ01000049; SNT18499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239KLM5; -.
DR   OrthoDB; 9794294at2; -.
DR   Proteomes; UP000198304; 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   3: Inferred from homology;
KW   Competence {ECO:0000256|ARBA:ARBA00023287};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198304};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT   DOMAIN          11..146
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   217 AA;  24723 MW;  9469A8E7588233FA CRC64;
     MQYIIDHIPE NTRCNRRPGT KMVPSSITIH NTGNPTSKAR DERGWLTNPT NTRTASWHIV
     IDEEEAVEAI PLNEIAWHAG NYEGNRTSIG IEVCESGDQE KVWQNVVYLT AKLLFERGWG
     VEQVKTHQNW SGKYCPRLIL PKWDKFLQDV EAELKNLSSD NQSNHASSNS QASSWAISAQ
     KWVMENRISD GTNPKTPATR EQIWVMLYNL MGGKEND
//
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