ID   A0A1F6S305_9BACT        Unreviewed;       525 AA.
AC   A0A1F6S305;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=A2359_00435 {ECO:0000313|EMBL:OGI27267.1};
OS   Candidatus Moranbacteria bacterium RIFOXYB1_FULL_43_19.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1801649 {ECO:0000313|EMBL:OGI27267.1, ECO:0000313|Proteomes:UP000178778};
RN   [1] {ECO:0000313|EMBL:OGI27267.1, ECO:0000313|Proteomes:UP000178778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGI27267.1}.
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DR   EMBL; MFSH01000015; OGI27267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6S305; -.
DR   STRING; 1801649.A2359_00435; -.
DR   Proteomes; UP000178778; 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; 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; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..525
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009526417"
FT   DOMAIN          50..200
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          67..217
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   525 AA;  57628 MW;  6E277F48382EB880 CRC64;
     MQRKKKKQNF IFSALIVFLV FSFGCSFSGA DMSRAEAAFV KKKQAETEVP KIYPRSSWSN
     AKYDKRSKKV WPAKYEDPKI IIVHHTATNY KNSTSKQIKK IYKYHSYTRK WGDIGYNYII
     GKDGSIFEGR YGGNGVVGGH SYFNGTNYNE GSIGIAILGN YENENLSSAA QSSLEKLIGW
     LAANNGISIK SSIKFHSKSL DNAVVGHRNV AGTACPGKNI YNLMSEIRIS AENLAGVFGS
     YAYQIPGDGE VYEMTGGKRY SASAKSPIVK ISEKQLQLFS LGGAAAVSRE YSYPSGTLFL
     SAGRRALLEN GALRLISGNA LLNSSYNPSS FVEIADEKWT GYATGTAAGF RSGAFVKDSG
     GNYFIISGNQ KRKIVLSSEE LKLIELGSAH EISPSESALY AEGENIASAA AFSEGTLMTK
     NNKNYYYITA DGKKKIVTKN VFRATFSQEM AVKVSIKLLK KYKTGKKLSF QNGAAVKYGK
     KYYFIENGKR RQFASKNIAA SMGYQNFQKA KKSEMSGIGN GEKIE
//