ID A0A0G0EDC4_9BACT Unreviewed; 256 AA.
AC A0A0G0EDC4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, 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=US16_C0042G0002 {ECO:0000313|EMBL:KKQ04928.1};
OS Candidatus Moranbacteria bacterium GW2011_GWE2_36_40.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618713 {ECO:0000313|EMBL:KKQ04928.1, ECO:0000313|Proteomes:UP000033827};
RN [1] {ECO:0000313|EMBL:KKQ04928.1, ECO:0000313|Proteomes:UP000033827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ04928.1}.
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DR EMBL; LBRX01000042; KKQ04928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0EDC4; -.
DR STRING; 1618713.US16_C0042G0002; -.
DR Proteomes; UP000033827; 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}.
FT DOMAIN 113..247
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 61..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 256 AA; 28554 MW; C75745898C26347F CRC64;
MCFLAIASLY FGLKGLQESK KTVQIQTNAA DFQENNNNPQ TENELQANEK SIEDGKIEIA
ENQEGEMVES KIPEKTNQPA DEEKKIETKK TDPPVDEEKN AKAGKIVDKL ISWGFTKSSG
RTIDSIIVHS SYDALGSDPY SVSGIIAEYK LYNVSAHYLI ARDGVIYRLV SDQNIAWHAG
VSKVPDGRTN VNDFSIGIEM INTESGKYTT EQYSALNSLI ATLTNKYKIK YILGHNEIAP
GRKTDPWGIE WSKVDR
//
