ID   A0A2A2GAP8_9BACT        Unreviewed;       493 AA.
AC   A0A2A2GAP8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=CK503_06350 {ECO:0000313|EMBL:PAU94418.1};
OS   Aliifodinibius salipaludis.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX   NCBI_TaxID=2032627 {ECO:0000313|EMBL:PAU94418.1, ECO:0000313|Proteomes:UP000218831};
RN   [1] {ECO:0000313|EMBL:PAU94418.1, ECO:0000313|Proteomes:UP000218831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN023 {ECO:0000313|EMBL:PAU94418.1,
RC   ECO:0000313|Proteomes:UP000218831};
RA   Liu D., Zhang G.;
RT   "Aliifodinibius alkalisoli sp. nov., isolated from saline alkaline soil.";
RL   Submitted (AUG-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}.
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:PAU94418.1}.
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DR   EMBL; NSKE01000004; PAU94418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2GAP8; -.
DR   OrthoDB; 2812205at2; -.
DR   Proteomes; UP000218831; 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; 2.60.40.4070; -; 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; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
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; PF18962; Por_Secre_tail; 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   Reference proteome {ECO:0000313|Proteomes:UP000218831};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..493
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013036505"
FT   DOMAIN          216..363
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          231..381
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   REGION          196..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  54808 MW;  B382AF3D5A0C3C45 CRC64;
     MDLVRQVFFC FIVIFFLPMG ADALQANSNQ SGLAEDSSKI KTEYINFDFG TTQKLKSVDN
     ANQTVQGIQA ADVDQQAILV SDEIVVPVEG ITPFLAVGSR LIQELAEKES DDIQLQIRSS
     TDYQQWSEWM TVHRDEHLTI HQDTVVGRLQ YLPKNTRSIQ FRVVIDDAGS SSLLRSMRLS
     FTSPGATSAE TLQALEETAS QQPRHNKSEI EDYPMPDYAT RSDWDCPDGQ DPSGSVSRTD
     VTHQIVHHTA GTNSSSDWPA VVRSIWDYHV NTNGWSDIGY NWLIDPIGVI YQGRGWINGD
     DEVQGAHFCG TNSNTMGVAL LGNFEETSPS LEALGNLEEL LAWKSDEKNI DPSAREYHSS
     SGLNLHTISG HRDGCSTLCP GENLYVRLPE VRENVDAKVG EAADTEGELV LESNYPNPFS
     ESTTINFSLE KAGNVQITIW DIAGRKVNEV TDQFYEADSH SESWNASGYA SGVYFCRLEF
     EDQAIIQKMV LLK
//