ID A0A1V4EEB4_9ACTN Unreviewed; 642 AA.
AC A0A1V4EEB4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=B1R27_00765 {ECO:0000313|EMBL:OPG11054.1};
OS Streptomyces sp. GKU 895.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1662404 {ECO:0000313|EMBL:OPG11054.1, ECO:0000313|Proteomes:UP000190311};
RN [1] {ECO:0000313|EMBL:OPG11054.1, ECO:0000313|Proteomes:UP000190311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GKU 895 {ECO:0000313|EMBL:OPG11054.1,
RC ECO:0000313|Proteomes:UP000190311};
RA Kruasuwan W.;
RT "Draft genome sequence of plant growth promoting endophytic Streptomyces
RT sp. GKU 895 isolated from root of sugarcane plants.";
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 -!- 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:OPG11054.1}.
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DR EMBL; MWJO01000001; OPG11054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4EEB4; -.
DR Proteomes; UP000190311; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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 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 SMART; SM00644; Ami_2; 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}.
FT DOMAIN 257..395
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 642 AA; 67585 MW; 6BAFD6AD2D266029 CRC64;
MHRRKRAVGV PVGIAVSALV AGSLLTLPGH ALADDPSASA NARQQALLAA AEEFDIPSSV
LLALSHQESA WEGHGALPST DGGYGPMNLT DVTPTMLAAG DAGAAGRADL DSLAADPALH
TLRQAAELTG LSVKSLREDD TTNIRGGAAL LASYEKELLG ATPADPSQWY GAVARYSQAK
QEQAAASFAD RVFRTIRSGA SATTQDGQRI RLSAGPSVAP AREQIHSLRL KTSSTAVATE
CPTTVDCTFV TGSPAGRQVA DRPANGIRID TIVIHDLEST YDAGVTGLAN PSNPAATHYV
MSSAGAVTQM VPTKDTAFHA GNYSTNLHSI GIEHEGYAAH GAAWYSEAQY QATADLVKYL
AARFDIPLDR QHIVGHDNVA GPNSALVSGM HWDPGYAWDW NHFMSLLGAP VSGVSEVPQP
GSVVSIKPSF ADNVQTLQVC PSDDPTGQTP TCIEQQHPTN FVYLHTAPSE TAPLFGDQAI
HGTAPGTDRV NDWGSTAQAG QQFVVADVQD DWTAIWFSGA KVWFHNPGGV STRTSYGVKI
IRPAGTTPVS LYGSSYPDKA EYPAGLGAST QAPLSMYAIP TGQAYVATRE PVATDDYFPS
SSAVVIGSKK MYTIQYNHRV ALVYANDVTA TTAVHHWEND GS
//