ID A4F641_SACEN Unreviewed; 366 AA.
AC A4F641;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=SACE_0163 {ECO:0000313|EMBL:CAL99515.1};
GN ORFNames=A8924_0548 {ECO:0000313|EMBL:PFG93314.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99515.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAL99515.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAL99515.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG93314.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93314.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-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}.
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DR EMBL; AM420293; CAL99515.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG93314.1; -; Genomic_DNA.
DR RefSeq; WP_009944960.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4F641; -.
DR STRING; 405948.SACE_0163; -.
DR KEGG; sen:SACE_0163; -.
DR eggNOG; COG5479; Bacteria.
DR HOGENOM; CLU_018529_0_0_11; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; 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; 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:UP000006728};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..366
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011934018"
FT DOMAIN 174..321
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT REGION 24..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 38169 MW; AAA638582FCCE77C CRC64;
MRLGLSFPCV LLLTAALATS VRAEPPEAPA GGTAVVPLGE TPSRGGQREV RLDQPFSMVG
LTWSGEAPDR VELRPLTEGG WGAWTEAELT SARGSEPVWT GRTTGVQVRA TRGGDDVTGE
LRLVALRPSL GRTPVAAAPK APAGRSAEPS AAPSPVPEAP SSTTATPRHA SAPPPLVRRA
DWGADERNMK WTPQPTETRA ATVHHTAGTN DYGCADSAAI VRGIFEYHAV HLGWGDIGYH
ALVDKCGTIF EGRAQGLERD VIGGHAMGFN PNTFGVAMLG NFQDVVPTSD ALTAAGAIIG
WKLRESGVAP DSAVELVSTG GEGSLHPPGA AVRLPAIFAH RDVGQTLCPG QLAYDRLDEI
RSAALN
//
