ID A0A238UQ77_9ACTN Unreviewed; 681 AA.
AC A0A238UQ77;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ORFNames=SAMN06264365_10118 {ECO:0000313|EMBL:SNR24196.1};
OS Actinoplanes regularis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=52697 {ECO:0000313|EMBL:SNR24196.1, ECO:0000313|Proteomes:UP000198415};
RN [1] {ECO:0000313|EMBL:SNR24196.1, ECO:0000313|Proteomes:UP000198415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43151 {ECO:0000313|EMBL:SNR24196.1,
RC ECO:0000313|Proteomes:UP000198415};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR EMBL; FZNR01000001; SNR24196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238UQ77; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000198415; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198415};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..681
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012669652"
FT DOMAIN 189..337
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
SQ SEQUENCE 681 AA; 70776 MW; DA668605A1638DE7 CRC64;
MRRNRFVAAI AAATPAVALA IVALSSSTPD PLLQTFPLAP AGAGLRLVAE TRGEVAELPE
RATKRFSLVG VTWDDPKAAA DGTIQVRTRP AGDRNWTPWR ALETDAPDAS GGVDGARVRG
ASDPLWVGPS DGVQARVVDA DGARELPAGL RVDLINPEAA TSARQEMVPV ADRQPRRING
VEIPARATPR MLTRTGWGAD EKIVTEAPTY TGPVEVFFVH HTATGNDYSC ASSTSIVRGI
EAYQVKSKGW NDIGYNFLVD KCGTIFEGRR GGVDRNVLGA HTLGFNTNAS AVAVIGDYRS
APISAAARLS VAQLAAYKLG AAGNAPAEQV AVTSGGGAKF AVGKRVILNR ISGHRDAGVT
ECPGDALYAQ LPAIRELAGG APTGLRVAKV TGAVPWGATY FTRGAVTPLW VLTTPTQLLN
RFDVYVDGAL ALSRAGGTRV GSLQLRPGLH HVAVQAVHLS GRTTTVTAKV YADVAPPAFT
TLPAVSLTAG TVGSTAPIRL DWSATDPSGV GSVVVSGTSE ASLDGDARSL TGTARVGARD
EWTVAATDHA GNRRTASFSR TPVVLQESAA TPTGSWRAVS GSGHLGGAAA LAASAASALS
WTFTGQSVGL VAAMSRTAGR VKVYIDNEFQ GYADLRSTSA QYRRVVFTKS WPDTAVHTVK
VLPEGTAARP AVTVDGLVYL R
//
