ID A0A1A2GKL3_9MYCO Unreviewed; 546 AA.
AC A0A1A2GKL3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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=A5764_20710 {ECO:0000313|EMBL:OBG29957.1};
OS Mycobacterium sp. 852002-51057_SCH5723018.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834094 {ECO:0000313|EMBL:OBG29957.1, ECO:0000313|Proteomes:UP000092171};
RN [1] {ECO:0000313|Proteomes:UP000092171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852002-51057_SCH5723018 {ECO:0000313|Proteomes:UP000092171};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL Submitted (JUN-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}.
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:OBG29957.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LZIR01000006; OBG29957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A2GKL3; -.
DR STRING; 1834094.A5764_20710; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000092171; 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; IPR013207; LGFP.
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 Pfam; PF08310; LGFP; 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 202..350
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT REGION 93..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 56988 MW; 56030A40738ADAB9 CRC64;
MLLTAIAATV VIVSWVGDAI HGGGAPTRPR AGDTQLAEQP LIGLGGGVTV RELSQATPFS
LVALTGNLAG TSIRVRAKRS DGSWGPWYQT EYETAAPDGG PAGTEGLAAG PSEGPRSTDP
VFVGTTTTVQ IAVTRPIDAP VTQPPPAPSS VSADNGGLGY KPASKEQPYA QNISAILISP
PQAPAKTHWT PPAGVLMPGQ APAIISRAEW GADESLRCGS PQYDNGVRAA VVHHTAGSND
YSPLESAGIV KAIYTYHSKT LGWCDIAYNA LIDKYGQVFE GSAGGLTKAV EAFHTGGFNR
NTWGVAMIGN FNDVPPTPIQ LRTVGRLLGW RLGLDGVDPK GTVALESAGS HYTTFPAGAI
ATLPTIFTHR DVGNTDCPGN AAYALMDEIR DIASHFNDPP EELIKALEGG AIYEHWLAIG
GMNSVLGAPT SPEDSAEGDA RYVTFAKGAM YWSPETGAQP ITGAIYDAWA SLSYERGPLG
LPTSAEIQEP LQITQNFQHG TLNFERLTGN VTDVVDGITT PLSTQSPSGP TVPPEHFSLP
SHPAAT
//
