ID A0A1C5EHG4_9ACTN Unreviewed; 796 AA.
AC A0A1C5EHG4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=GA0115254_126660 {ECO:0000313|EMBL:SCF94654.1};
OS Streptomyces sp. Ncost-T10-10d.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839774 {ECO:0000313|EMBL:SCF94654.1, ECO:0000313|Proteomes:UP000198750};
RN [1] {ECO:0000313|Proteomes:UP000198750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ncost-T10-10d {ECO:0000313|Proteomes:UP000198750};
RA Varghese N., Submissions Spin;
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}.
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DR EMBL; FMDF01000218; SCF94654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5EHG4; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000198750; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR013783; Ig-like_fold.
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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 42..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 296..444
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 311..477
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 81590 MW; 820DC9E6FF5C6ABF CRC64;
MRGSTRTPHW SPRDQLSPAA APDEPNVRKR SLGYDLRSKR RIWITAALAT SAVAGALVFE
GVTGNSSVDA DAKSGPTKAD VHATALKVDG DGTSATLGKR DTKPFSMLGI TWTDAAAKVT
GAVEVRTRSA ANGNWTSWLP LETDIDGRTE AGRSGVRGST EPRWVGPSNG VEVRINAGGK
VSAKLPAGLR LDTVDPGRSG TLNADPAAFA ADIPAADATT DPSADPSDPA ATEPPAPSDS
TEPPAEVTPS DPASPSPSDS ATVQPTPPVS PSPSAPASAS PTDTLPPAPS STVPKPPITS
RAGWGADESI SPEAPEYTDT VKAVFVHHTA GTNTYSCADS AAVVRSVYAY HVQANGWKDI
GYNFLVDKCG TVFEGRKGGV DRPVFGAHTY GFNRQTAGIA VLGTYTDTTA PSAVTTSVAR
IAAWKLGQYK GDPAGSTMLT AGATGSNLAG TKFTAGTQYS FKQISGHRDG FATECPGTKL
YGQLPAIRSL AAGPVTGLAV KSVTGAGLSG TTYYTKSTVT VGWSATTPSA FISKYELLVD
GKSVATTTGT ATSAKATLAV GSHQVQVRAT HQSGKVTTSA AATVVADQTA PAFTTKPNLA
LGTGTVNTTA VPITLKWKAT DAASLKEVRL TAPLAKTYGP TTTSASHTAK SGVATSWAMT
AYDQAGNTAA ASVSGTPVIV QESSATKTGT WTTKSSSSYL GGKSYSSSSK SASLSWTFTG
RSVALVASRA ATSGQVYVYV DGVKVSTVDL KSSTTKYRDA LWTKSWSSSA KHTVKIVVVA
TSGRPTVTTD GIVYLK
//
