ID A0A0M8TS22_9ACTN Unreviewed; 655 AA.
AC A0A0M8TS22;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ADK57_13930 {ECO:0000313|EMBL:KOU69112.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU69112.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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}.
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:KOU69112.1}.
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DR EMBL; LGDG01000122; KOU69112.1; -; Genomic_DNA.
DR RefSeq; WP_053749740.1; NZ_LGDG01000122.1.
DR AlphaFoldDB; A0A0M8TS22; -.
DR STRING; 1415546.ADK57_13930; -.
DR PATRIC; fig|1415546.3.peg.3035; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000037741; Unassembled WGS sequence.
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; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
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 SMART; SM00644; Ami_2; 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:UP000037741}.
FT DOMAIN 285..422
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 103..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 69575 MW; 971D63EE91185C5F CRC64;
MRGSATAIDR AAGHRRIRRT AGAVGSAALL LPLLGAAPSD ARDSAAGLQQ AFASAAAEYH
VPQSVLLGVS YLQSRWDAHA GAPSVTGGYG PMHLTDARTA LAEAPPHHSE GTEDARGDGA
RTPLHPEAKV PENSELPARL KTLSKAAELT GLPAERLRTD PAANVAGGAA LLAAAQKDLG
EPLSKDPADW YGAVARFSGA DDSATGAAYA GDVYDVLRTG AERITDAGQQ VALAAQPGLA
PETAQLARTG LRTLDASGTE CPTTVSCEWI PAPYEEFGEG DYGNHDLGNR PASQSIDYII
VHDTEGAWEG VLDLVQDPTY VSWNYSLRST DGHIAQHVKA KDVAWHAGNW YVNAKSIGLE
HEGFLANPDA WYTEAMYRSS ARLVKYLSKK YGVPLDRQHI LGHDNVPGPT TSTVGGMHTD
PGPYWDWGHY FALLGRPFEP SAGKDGGMVT IRPDYATNQP GYTGCVAQGE PCAAHGSSAV
RLYSGPAESY PLIKDIGLGT TPTTGVNDLS SRVSTGQQYA VAGRDGDWTA IWYLGQKAWF
KNPKKHPTAV NATGLVVTPK DDLTSIPVYG RAYPEASAYP AGVPAQSVSP LPYKVLADQK
YVVGGKVPGQ YYYAVTFDEA SHQVVVGKDL YYEIQFGHRV AFVRAADVRE ERSAG
//
