ID A0A1V4A1T0_9ACTN Unreviewed; 458 AA.
AC A0A1V4A1T0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=B1H18_27785 {ECO:0000313|EMBL:OON73039.1};
OS Streptomyces tsukubensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83656 {ECO:0000313|EMBL:OON73039.1, ECO:0000313|Proteomes:UP000190539};
RN [1] {ECO:0000313|EMBL:OON73039.1, ECO:0000313|Proteomes:UP000190539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F601 {ECO:0000313|EMBL:OON73039.1,
RC ECO:0000313|Proteomes:UP000190539};
RA Zong G., Zhong C., Fu J., Qin R., Cao G.;
RT "Draft Genome Sequence of Streptomyces tsukubaensis F601, a Producer of the
RT immunosuppressant tacrolimus FK506.";
RL Submitted (FEB-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:OON73039.1}.
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DR EMBL; MVFC01000033; OON73039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4A1T0; -.
DR STRING; 83656.B1H18_27785; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000190539; 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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000190539};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..458
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038598898"
FT DOMAIN 263..411
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 277..438
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 49..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 47259 MW; 2471A544D30978FC CRC64;
MRGFLASSIG VTCAAALAVP LAFPSGARTT ARAATDRSVS EESADIVPGA TRSLRMAPLP
GDRAGGASSA EGTARREVRP FSLVGVVWDD AEKELHGRVQ VRTRATGGGA WSGWQDLETH
NAEHAADRDT PEGARGAAHG STAPLWVGPS DAVESRVTPE RAGGEGEAAG RAGAKRTGTG
LPAGLRLDLV DPGEGSAAGA GGASGMEGAS GAEGAEGMEA ASGTEGAEGP EGAGGPAAPL
GTLSADGDRA GAAPVRSHTG PRPAIVTRKR WGANERLREK KFRYTRTVKA AFVHHTATGN
SYTCAQAPSV IRGIYRYHVK SMGWRDIGYN FLIDKCGKIY EGRAGGVTKP VMGAHTLGFN
TNSTGIAVIG TYSRAKPPAA AVKGVARLTA WKLGLTGANP KRKVTLVSGG SNRYHKGKKV
RMNVISGHRD GFSTECPGAR LYKKLGTVRS TAAKRQHR
//
