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Database: UniProt
Entry: A0A1V4EEB4_9ACTN
LinkDB: A0A1V4EEB4_9ACTN
Original site: A0A1V4EEB4_9ACTN 
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
//
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