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Database: UniProt
Entry: A0A164HV14_9NOCA
LinkDB: A0A164HV14_9NOCA
Original site: A0A164HV14_9NOCA 
ID   A0A164HV14_9NOCA        Unreviewed;       276 AA.
AC   A0A164HV14;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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=AWN90_13725 {ECO:0000313|EMBL:KZM68843.1};
OS   Nocardia terpenica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM68843.1, ECO:0000313|Proteomes:UP000076512};
RN   [1] {ECO:0000313|EMBL:KZM68843.1, ECO:0000313|Proteomes:UP000076512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM68843.1,
RC   ECO:0000313|Proteomes:UP000076512};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KZM68843.1}.
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DR   EMBL; LWGR01000021; KZM68843.1; -; Genomic_DNA.
DR   RefSeq; WP_067580796.1; NZ_KV411303.1.
DR   AlphaFoldDB; A0A164HV14; -.
DR   STRING; 455432.AWN90_13725; -.
DR   OrthoDB; 5178799at2; -.
DR   Proteomes; UP000076512; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076512}.
FT   DOMAIN          32..167
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   276 AA;  29761 MW;  6112BAFE3699303D CRC64;
     MPWNGDPSWL ADVIRAEGVE VREWRDPDGT PWQQIGHGDF GNVWGVLWHH MGVNDQGANV
     IRNGVPGLDG PIANIHLSRD GVATIVSGGV AWHAGLGSWP GVPTNNGNFH LIGIEMAGNG
     TDPWPAKCWD AAVKIGAAIS RRLGYGADRN IAHKEYAGAA QGKWDPGNWD MDAFRNQIQN
     RLDRGAPQED VLDMTPEQLK ALIFECLDTY VGPIGSDVKD IRWQLVGARD NIPGDIGLSY
     PGHQFFGKGR TLDDAVAAIG EKLGVDGMHD PKAGGK
//
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