ID A0A1G7BCD3_9FLAO Unreviewed; 217 AA.
AC A0A1G7BCD3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN05421636_10491 {ECO:0000313|EMBL:SDE24577.1};
OS Pricia antarctica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pricia.
OX NCBI_TaxID=641691 {ECO:0000313|EMBL:SDE24577.1, ECO:0000313|Proteomes:UP000199109};
RN [1] {ECO:0000313|EMBL:SDE24577.1, ECO:0000313|Proteomes:UP000199109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23421 {ECO:0000313|EMBL:SDE24577.1,
RC ECO:0000313|Proteomes:UP000199109};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNAO01000004; SDE24577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7BCD3; -.
DR STRING; 641691.SAMN05421636_10491; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000199109; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199109}.
FT DOMAIN 46..181
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 217 AA; 24958 MW; 3CF1DBA634661E87 CRC64;
MKNFLIPILF VLLHVSCKPQ VEIIDKPIIF DETRRELTLE YLKDHYGLDQ DAPTIDPKMI
VLHWTAIPTF EGSFDAFKNV KLPSWRPDLE NASALNVSSH FLIDQDGTIY RLMPETTMAR
HVIGLNHTAL GVENVGGTEG KPLTKAQLKS NIGLVEYLAA KYKIDYLIGH YEYRNFENHP
LWLEKDDGYR TKKTDPGVDF MQKVRQATQN LNFKQNP
//
