ID A0A0B5ERM9_STRA4 Unreviewed; 712 AA.
AC A0A0B5ERM9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SLNWT_1030 {ECO:0000313|EMBL:AJE81406.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE81406.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE81406.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; CP010519; AJE81406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5ERM9; -.
DR KEGG; sals:SLNWT_1030; -.
DR Proteomes; UP000031523; Chromosome.
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 CDD; cd06583; PGRP; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.40.128.340; -; 3.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
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 Pfam; PF13517; FG-GAP_3; 2.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 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:UP000031523};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..44
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 45..712
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002114777"
FT DOMAIN 254..382
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 211..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 74963 MW; 9F96D7B40564A48D CRC64;
MNRDRRTTRS ALGTTRRSAT RLRRTLFGGL LGACLALPAL PATATGAPAP EPTGEGRTAA
AFREAARASE VPRDLLVALG YSETHLDGHD GKPSQARGYG VMHLTDNPDQ HTLRTAAELT
GLDPAALRRD TRANIRGAAA VLREYADDLG LDAAERRDPA AWYPAIARYS GAGNDSTARL
YADAVYTFLA QGVRARTPEG EQLGVPRQRI TPDRGRYEDV PSLDARPATG GKQTADASVL
SEDYPPARWI PAAAGNYARG RSAAIRTIVI HVTQGSYAGS ISWFQNPASG VSAHYILRSS
DGEVTQMVRD GDTAYHARSA NPSALGIEHE GYVSDPSWFT DAMYRSSAAL TRHLADRHGI
PKDRAHIVGH NEVPGNDHTD PGPHWNWNYY MSLVQSGGGL KLGGSPTDFS GDGKADVVTF
THGAAADVYA ATSTGAGFSG TTVKWNDYFA LSGEVPSSGD FDGDGKDDIV TFTRGSLADV
YVGLSSGSAF AGGVKWNDFF AVGGEVPATG DFDGDGKDDI VTFTNDANGD AFVALSDGAK
FGAGVKWHDF LAPNGEFPAV GDVNGDGKDD VVVFTQGTRG DVFVALSTGS GFAPAQLAHE
FFAPGAEQPR VGDVNGDGKD DIVTFTSNAD RDVYVALSDG SKFGPGVKWN DSFTPAGEFP
YVGDFDGDGK DDIVTFTKNA SADVYVGLST GSSFGAGAKW HDLFGLPGET AF
//
