ID A0A1B8ZW99_9FLAO Unreviewed; 341 AA.
AC A0A1B8ZW99;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=BBI01_03875 {ECO:0000313|EMBL:OCA75849.1};
OS Chryseobacterium artocarpi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1414727 {ECO:0000313|EMBL:OCA75849.1, ECO:0000313|Proteomes:UP000092651};
RN [1] {ECO:0000313|Proteomes:UP000092651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTM-3 {ECO:0000313|Proteomes:UP000092651};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:OCA75849.1}.
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DR EMBL; MAYH01000012; OCA75849.1; -; Genomic_DNA.
DR RefSeq; WP_065393526.1; NZ_MAYH01000012.1.
DR AlphaFoldDB; A0A1B8ZW99; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000092651; 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;
FT DOMAIN 93..235
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 341 AA; 38403 MW; CC1D8AEDE887E9FF CRC64;
MRKTLYIIGL STLVFSCASQ KNVKKNTYQP KTPVVQPKTV VKTQTQEVQK PKVVSDHGVD
FFTTNIADPT KNDNTASYGS IVSAKPAGYK VVKTYFPAMA QNFRQRYLIL HYTVLPDDKS
ITVLTQPGVS AHYLVNNTGD NEIYQLVDEN KRAYHAGVSA WKADKNINDT SIGIEIVNPG
FTTDATGKRV FVPFSDAQIR KVAALAKDIV TRYQIPATNV LGHADIAPTR KQDPGPMFPW
KKLYDEYQIG MWYDEGLKSN YQEIAQADFA TKYIDPTFIF SIQTALQKFG YGIELSGKWD
DATKKTIEAF QYHFRPQNFD GIMDAETYAI LQALNVKYSI K
//
