ID A0A1Y3X7Y8_9FIRM Unreviewed; 250 AA.
AC A0A1Y3X7Y8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=B5G06_13015 {ECO:0000313|EMBL:OUN78180.1};
OS Flavonifractor sp. An52.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Flavonifractor.
OX NCBI_TaxID=1965642 {ECO:0000313|EMBL:OUN78180.1, ECO:0000313|Proteomes:UP000195424};
RN [1] {ECO:0000313|Proteomes:UP000195424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An52 {ECO:0000313|Proteomes:UP000195424};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
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}.
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:OUN78180.1}.
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DR EMBL; NFIB01000045; OUN78180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3X7Y8; -.
DR Proteomes; UP000195424; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000195424}.
FT DOMAIN 8..158
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 250 AA; 27363 MW; 05016E123DE2FBFC CRC64;
MHITEHILTN SDCYKAGRTI KPKGIMVHST GVAQPDVNVF LKAWDKPGVN ACVHAIVHRG
GVTETLPWNW RGWHAGGAAN NTHISFEILE PAGHTYKGGA MIGYDPIKNK AYFQQVYDTA
VELCAYLCEK YGLDPERDII DHAEGCKLGL ASNHSDVGQW FPKHGKSMDT LRADVKARLK
GGEPEMTQEQ FDAAFTAHEG EISARTVSEW AKEAWNKAKD AGVFDGTAPG APLTREQAAL
ILERLGLLGK
//