ID A0A2T5AZ99_MYCDI Unreviewed; 257 AA.
AC A0A2T5AZ99;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JAN-2026, 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=C7449_108114 {ECO:0000313|EMBL:PTM92066.1};
OS Mycoplana dimorpha.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Rhizobiaceae; Mycoplana.
OX NCBI_TaxID=28320 {ECO:0000313|EMBL:PTM92066.1, ECO:0000313|Proteomes:UP000241247};
RN [1] {ECO:0000313|EMBL:PTM92066.1, ECO:0000313|Proteomes:UP000241247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7138 {ECO:0000313|EMBL:PTM92066.1,
RC ECO:0000313|Proteomes:UP000241247};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) 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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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:PTM92066.1}.
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DR EMBL; PZZZ01000008; PTM92066.1; -; Genomic_DNA.
DR RefSeq; WP_108004345.1; NZ_JBHEEX010000004.1.
DR AlphaFoldDB; A0A2T5AZ99; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000241247; Unassembled WGS sequence.
DR GO; GO:0019867; C:outer membrane; IEA:TreeGrafter.
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 GO; GO:0009254; P:peptidoglycan turnover; IEA:TreeGrafter.
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; IPR051206; NAMLAA_amidase_2.
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 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.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000241247}.
FT DOMAIN 16..153
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 257 AA; 28084 MW; 5096AB8CBCB46D71 CRC64;
MTAFEPDFPG AAVVPSPNHG ERRDGRRPDA IILHYTGMES TDGALAWLCA EESEVSSHYF
VYEDGRIAQL VPESRRAWHA GKSNWKGETD INSCSIGIEI ANPGHPGGLP DFPEAQIAAV
VELCRNCGER WRIAPERVLA HSDVAPIRKV DPGEKFPWER LHAAGIGHWV EPAPIAGGRF
FQRGDEGAPV EALQAMLALY GYATEITGIF DVATEGAVAA FQRHFRPARV DGIADSSTID
TLHRLLKRLP VRNGFTA
//
