ID   A0A1G9SLM7_9ACTO        Unreviewed;       739 AA.
AC   A0A1G9SLM7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN04487766_10213 {ECO:0000313|EMBL:SDM36413.1};
OS   Actinomyces ruminicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=332524 {ECO:0000313|EMBL:SDM36413.1, ECO:0000313|Proteomes:UP000199671};
RN   [1] {ECO:0000313|EMBL:SDM36413.1, ECO:0000313|Proteomes:UP000199671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPR-7B {ECO:0000313|EMBL:SDM36413.1,
RC   ECO:0000313|Proteomes:UP000199671};
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   -!- 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; FNHU01000002; SDM36413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9SLM7; -.
DR   OrthoDB; 514320at2; -.
DR   Proteomes; UP000199671; 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; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR028994; Integrin_alpha_N.
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; SM00644; Ami_2; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..739
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011638422"
FT   DOMAIN          296..442
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          308..475
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   REGION          214..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  75371 MW;  B3778403E05A45B8 CRC64;
     MRVRRLLGLS AVVPLLAAGL MPATSAVADT AEAAAPVQLL ELTTSTGEAT EVAEAGLVET
     ASAGTSGGTG VAPELASRLA AVARAAAAGG VDPEADALLL TEPLEVADFL VAGFTWTGAD
     DLPDGLDVYL RVREDGVWSD WYLNEASGAG RDDGTGVVGT EEFITGGADA VQASVVGDAA
     QLPAGLQLAL IPGRPVGEEV LDPADLETAD AEPTALATPA EAPQDPTSGL TTPSPDVATQ
     NADEAAPQGE EPEPADTQTA TAEPGAGSSG TSGGTSVSPG LPAVLAAATT AGGLPVPVIT
     RSEWGASSSY MSWSPEYAAA KHVIVHHTAG TNNYTSSQSA SIVNGIYYYH AVTLGWGDIG
     YNFLVDKYGQ VFEGRYGSTG AAAGKMVVGG HAYGANTGTM GISMMGTYTS VSPSSTQLTN
     VGKMAGWFLG RAGITSATGS ASFTFKSTEK YAAGQTVSLP AISGHRDVGY TACPGDAGYS
     KLGQIRSAAQ NQINTSKGSG NPGSSTSTTS SSGARSHQIY LNDSWSATAN TVFTYTTPAT
     SVLAGDWNGD GVDSTGVRNG SSYGFRNTNT SGASLRTFTY GKSTDQVLVG DWDGNGTDTL
     AVRRGNTYFI KNSMYSGSAD KVVTYGNASD EVVVGDWDGN GTDTLAVRRG NTYYIKNSIT
     SGSADKVVAY GKSTDTVLVG DWNASGKDTL AVRRGNTYYI KNSITSGSAD RVQAYGKAND
     ELIVGDWDGD GSDTLGVTR
//