ID   A0A0G1FXW3_9BACT        Unreviewed;       886 AA.
AC   A0A0G1FXW3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=UW11_C0004G0018 {ECO:0000313|EMBL:KKT26988.1};
OS   Parcubacteria group bacterium GW2011_GWA2_43_9b.
OC   Bacteria.
OX   NCBI_TaxID=1618828 {ECO:0000313|EMBL:KKT26988.1, ECO:0000313|Proteomes:UP000034814};
RN   [1] {ECO:0000313|EMBL:KKT26988.1, ECO:0000313|Proteomes:UP000034814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT26988.1}.
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DR   EMBL; LCHB01000004; KKT26988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1FXW3; -.
DR   STRING; 1618828.UW11_C0004G0018; -.
DR   Proteomes; UP000034814; 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   InterPro; IPR013693; SpoIID/LytB_N.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF08486; SpoIID; 1.
DR   SMART; SM00644; Ami_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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          45..206
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          66..238
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   REGION          557..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..584
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  97708 MW;  944E6121BC46B409 CRC64;
     MERKILTKNI IWLFVFSLVL PNGLFFAKST NAQNEGLVYG DSDVPVILPR ASWDNTPALN
     ALMTWAPDKN ASPSDYQPVE RIILHDTGCD ASNPTCNNNQ NPVATIQAMY RYHAVTRGWG
     DIGYNYIIDQ QGRIYEGRYG GNGSRGAHVF VDKTKDNFNF GTIGITVLGN YGKIQPAEAV
     YQSLIRLVAW LAATNNLDPQ GTRSSSIWNF TTSEFSSLYN GPIVVGHKDV EKGNPDPGLL
     DVAKVRRATA DFAAKYRNYI YQVDSLPKIY KIGSGTRQIY NDLPTYVSMG GVYRGSVIIS
     QTQADLFSES RFLKYPDGSL LRIKDNFSVY LIQDGQKRNL NVSVKQFMVL GFDFDRVRVV
     EETDLAGYLE TDMVKYGPDK QLLSDGQRVY LIQAGQKRWI PSDALFATLG YSWSKIKSAP
     TDLKNYLDGA VLSYPDGTLL QAAGQEAVYL VSGGQLSRFI SAEIFLNLKY NWSKIKKIPA
     EELAYYPIGD FVKYKDGALL RPNDENNVYL ISGGKPQLVD GATFKKKKYK WVNVLVISAQ
     DFHILYRGAA IEQPISTQLS PSPSATPTPS LTPVPSPTPT IIPTPASSSS PISSSEPKMR
     VAVYEVTAPS VTLTANMPFN ILDKTGQIVV GKAANENYVY NISASSTAFV RIVPQSTDGI
     VQIVSYEDHP AWKPSLNYNQ FHGTMEIVYS AKSNKIWAVN ELRLEDYLKG IAEINQTDSA
     EHQKTMIVAS RTYAYYYILK GGKRGADEVY ILNNTSADQL YKGYTRELSA PAVVDAVNFT
     RGEVAVYNGA PIVTAYSSGA PELATSGTKN ACTVWGNQYC QAGFEYLAGE VKDPANAPYT
     QSVCGGGNHC VGLSAAGSRQ FSLTGAKNYQ EVLKYYYSGT EIKKIY
//