ID A0A240C661_SERFI Unreviewed; 255 AA.
AC A0A240C661;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiD_2 {ECO:0000313|EMBL:SNW03464.1};
GN ORFNames=SAMEA4384070_03320 {ECO:0000313|EMBL:SNW03464.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNW03464.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNW03464.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNW03464.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; LT906479; SNW03464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240C661; -.
DR STRING; 1411141.GCA_001590885_01514; -.
DR KEGG; sfj:SAMEA4384070_3320; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000215134; Chromosome 1.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
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.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SNW03464.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215134}.
FT DOMAIN 7..158
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 255 AA; 28378 MW; A147566C99D747FC CRC64;
MFKIDYNSYR SVASFGHRVR FLVLHYTAQN FVDSVQSLTG KSVSAHYLVP DPTDPGYQAA
GFSGVRIFNL VDENERAWHA GASQWGNRNN LNDTAIGIEI VNLASGDGED ITFPPFDPQQ
IAAVTRLAQN ILQRYPDITP VNVVAHSDIA PGRKSDPGPQ FPWRQLHQAG VGAWYDDAVK
QRHQQSYCSQ GLPAQQELLA LFAKYGYDTS AATNAEGYRQ LVRAFQLHFR QQKYDGVMDA
ETAAVLRALV DKYVA
//
