ID A0A1Y5S2N0_9RHOB Unreviewed; 243 AA.
AC A0A1Y5S2N0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiD {ECO:0000313|EMBL:SLN31318.1};
GN ORFNames=TRL7639_01316 {ECO:0000313|EMBL:SLN31318.1};
OS Falsiruegeria litorea R37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsiruegeria.
OX NCBI_TaxID=1200284 {ECO:0000313|EMBL:SLN31318.1, ECO:0000313|Proteomes:UP000193077};
RN [1] {ECO:0000313|EMBL:SLN31318.1, ECO:0000313|Proteomes:UP000193077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7639 {ECO:0000313|EMBL:SLN31318.1,
RC ECO:0000313|Proteomes:UP000193077};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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}.
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DR EMBL; FWFO01000001; SLN31318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5S2N0; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000193077; Unassembled WGS sequence.
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 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, ECO:0000313|EMBL:SLN31318.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193077}.
FT DOMAIN 30..163
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 243 AA; 26483 MW; 6654E5EABD94DE13 CRC64;
MPAPGIQHRS AVPSRTDASV DAEGAIWHPS PNCGPRRDGL TPSLVVVHYT AMQSAEAALE
RLCDPAAEVS AHYLIGQDGT LWQMVREADR AWHAGAGEWH GRCDINSRSV GIELDNRGDH
PFAEPQMATL ERLLPQILSR WGIASAGVIG HSDMAPGRKF DPGPRFDWQR LEQQGLAGGR
GHDCGPQNAP WDVFRALAQR AGFTADVDDA TLLSAVRLRY RPWGRGTLAP EDFSPLGQTA
LWT
//
