ID A0A108C6Y6_9BURK Unreviewed; 291 AA.
AC A0A108C6Y6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=WM16_23980 {ECO:0000313|EMBL:KWK69197.1};
OS Burkholderia ubonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=101571 {ECO:0000313|EMBL:KWK69197.1, ECO:0000313|Proteomes:UP000065504};
RN [1] {ECO:0000313|EMBL:KWK69197.1, ECO:0000313|Proteomes:UP000065504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB782WGS {ECO:0000313|EMBL:KWK69197.1,
RC ECO:0000313|Proteomes:UP000065504};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) 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:KWK69197.1}.
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DR EMBL; LPLU01000111; KWK69197.1; -; Genomic_DNA.
DR RefSeq; WP_060237344.1; NZ_LPLU01000111.1.
DR AlphaFoldDB; A0A108C6Y6; -.
DR Proteomes; UP000065504; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF10; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..291
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007129584"
FT DOMAIN 33..179
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 291 AA; 31250 MW; 66C7245298C63766 CRC64;
MRLFIRGAFC AGLCMLAACT SPSLVGRGTY FADTSRHAQG ADARIRFLVM HYTESDEAQS
LRTLTGDAVS AHYVVPAQPR IEWGKPVVYQ LVPEAQRAWH AGVSAWQGTT ELNAASIGIE
NVNGGPADTP QGRTWQPYPP AQVDALIRLS QDIVARYAIP PTRVVGHSDI APQRKIDPGP
AFPWRALAQA GVGAWPDDAT VVARLAGRDP HAAVDVRGLQ LKLARYGYDV PTDGVLDERT
RRVFAAFQMH FRPSGYAGDP DAESDAIAQA LLDKYFPGQA PAEDGAAPGA P
//
