ID A0A1W1UHR6_PEPAS Unreviewed; 159 AA.
AC A0A1W1UHR6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN00017477_0226 {ECO:0000313|EMBL:SMB80361.1},
GN SAMN00017477_2110 {ECO:0000313|EMBL:SMB93658.1};
OS Peptoniphilus asaccharolyticus DSM 20463.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=573058 {ECO:0000313|EMBL:SMB80361.1, ECO:0000313|Proteomes:UP000192368};
RN [1] {ECO:0000313|EMBL:SMB80361.1, ECO:0000313|Proteomes:UP000192368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20463 {ECO:0000313|EMBL:SMB80361.1,
RC ECO:0000313|Proteomes:UP000192368};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; FWWR01000009; SMB80361.1; -; Genomic_DNA.
DR EMBL; FWWR01000017; SMB93658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1UHR6; -.
DR STRING; 573058.SAMN00017477_0226; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000192368; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
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:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 9..149
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 159 AA; 18365 MW; E443871E196C691E CRC64;
MLIDKRPIKY NFSKRGMQRP VFIVVHDTGN TSVGADAIAH YKYFGRGDRQ ASAHYFVDEK
GAVEIIEVTN AAWHCGDGRG RFGITNSNSI GVELCVNQGN DWEKTKQNGI ELIKFLMDAY
GIPWERVVRH YDASKKVCPA RMSGNNWKEW WEFREMLRY
//