ID A0A1I2XWF5_9SPHI Unreviewed; 219 AA.
AC A0A1I2XWF5;
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=SAMN04489864_10683 {ECO:0000313|EMBL:SFH17820.1};
OS Pedobacter insulae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=414048 {ECO:0000313|EMBL:SFH17820.1, ECO:0000313|Proteomes:UP000199666};
RN [1] {ECO:0000313|EMBL:SFH17820.1, ECO:0000313|Proteomes:UP000199666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18684 {ECO:0000313|EMBL:SFH17820.1,
RC ECO:0000313|Proteomes:UP000199666};
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}.
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DR EMBL; FOPP01000006; SFH17820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2XWF5; -.
DR STRING; 414048.SAMN04489864_10683; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000199666; 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:UP000199666};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..219
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011733267"
FT DOMAIN 48..198
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 219 AA; 24996 MW; D4B5BE1A303A8E28 CRC64;
MRYQKILCLI LFCSPLVLSA QEIKIIDKPI IYDSTRIQLT LQYLKDRHGI NQKTVEIEPK
IIVLHWTASK TMLSAFNTFN KPTLDGGRKA IAGASNLNVS SQFLIDRDGS IYRLMPENVF
ARHVIGLNYC AIGVENVGSN DFPLTKEQLI ANEQLVRYLS KKYEITHLIG HYEYNQFKGT
KLWKETDPNY QTGKTDPGVA FMEKIRINLK DLKLKGASD
//
