ID A0A1J4PQV3_9ACTN Unreviewed; 633 AA.
AC A0A1J4PQV3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=VT52_033250 {ECO:0000313|EMBL:OIK23299.1};
OS Streptomyces malaysiense.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428626 {ECO:0000313|EMBL:OIK23299.1, ECO:0000313|Proteomes:UP000034838};
RN [1] {ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.H., Chan K.-G.;
RT "Genome sequencing of Streptomyces sp. MUSC136T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIK23299.1, ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces malaysiense MUSC 136.";
RL Submitted (OCT-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 -!- 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:OIK23299.1}.
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DR EMBL; LBDA02000116; OIK23299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4PQV3; -.
DR Proteomes; UP000034838; 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; 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:UP000034838}.
FT DOMAIN 245..382
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 62..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 68755 MW; BD4440073B7C333B CRC64;
MTDDDAPEQR LQIAFTDAAH DFHVPRSVLM SVSYVQTRWD AHPGSPSVAG GYGPMHLVDT
SRFPAASPTP GVQGGGALQP SAGAAGAPAA RPDGVLAGRS VKPADLQRAA RLTDVPAGRL
RTDAAANVRG GAALLAATQQ QLGKPLSEDP ADWWEAVERF PGTPDITSAA TYANDVFAVI
RKGAHRTTAE GQEVSLPASP SVRPHTVRTE KPRHAKGTEC PAEVSCDWLA APYVEIDDDG
DYGNHDLADR PRDQKIEYIV IHDTEARLSS MFQTVQDPTE ASWHYSIRSS DGHVTQHIQT
KDEAWHSGNQ YVNARSIGIE HEGFLRQPGT WFTEQMYRTS ARLVRYLAKK YGIPLDRQHI
FGHDNVPSPT GDSIPDMHDD PGPFWDWRHY FDLLGAPLKA TAGPNSDMVT ILPDYATHSP
KFTGCLKPGA PCPKHGSSAV RMYTRPDERA PLIQDPGRHP DGGESTLDVD DLGARASAGQ
TFAVAERRGD WTAVWYQGRK AWFKNPKKQA TAVGAAGKMV TPKAGLDEIP VFGRALPEED
AYPEGMEEEP EAPLPYHFRA GQRYVTEGTI DSSFVPRSAF VESPEPVVKG DETYYQIQFD
HRIAYVRSSD VDVVGSTVAA GPSSATRGGS TDN
//
