ID A0A150UIY4_9BRAD Unreviewed; 260 AA.
AC A0A150UIY4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SE92_30950 {ECO:0000313|EMBL:KYG24129.1};
OS Bradyrhizobium sp. AT1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=574934 {ECO:0000313|EMBL:KYG24129.1, ECO:0000313|Proteomes:UP000075342};
RN [1] {ECO:0000313|EMBL:KYG24129.1, ECO:0000313|Proteomes:UP000075342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT1 {ECO:0000313|EMBL:KYG24129.1,
RC ECO:0000313|Proteomes:UP000075342};
RA Okubo T., Minamisawa K.;
RT "Evolution of nitrogen fixation genes.";
RL Submitted (JAN-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 -!- 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:KYG24129.1}.
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DR EMBL; JXDL01000001; KYG24129.1; -; Genomic_DNA.
DR RefSeq; WP_063202091.1; NZ_JXDL01000001.1.
DR AlphaFoldDB; A0A150UIY4; -.
DR STRING; 574934.SE92_30950; -.
DR PATRIC; fig|574934.3.peg.6539; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000075342; 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 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:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 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.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 17..154
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 260 AA; 28237 MW; DFCE31EA7727A912 CRC64;
MRTFEPDSSI VSDIIPSPNH GERNKGRQPD MIVLHYTGMP DVEGALARLC TAGTEVSAHY
VVLEDGRIVQ CVPETRRAWH AGVSSWAGED DINSCSIGIE IVNRGHDWGY PEFPLRQIAA
VIALCRGIML RRKVPTHRVL GHSDVAPARK KDPGEKFPWH SLANSGVGHW VTPAPVVRGE
SLMLGTISDE VLSMQQALAK YGYGVPLSGK YDAATMEVVT AFQRHFRPAR LDGVADHSTL
STLQALLASL PAEGTTVASK
//
