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Database: UniProt
Entry: A0A011QVI3_9PROT
LinkDB: A0A011QVI3_9PROT
Original site: A0A011QVI3_9PROT 
ID   A0A011QVI3_9PROT        Unreviewed;       193 AA.
AC   A0A011QVI3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD {ECO:0000256|ARBA:ARBA00039257};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE   AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00042615};
GN   Name=ampD {ECO:0000313|EMBL:EXI93170.1};
GN   ORFNames=AW12_00026 {ECO:0000313|EMBL:EXI93170.1};
OS   Candidatus Accumulibacter sp. BA-94.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI93170.1, ECO:0000313|Proteomes:UP000020878};
RN   [1] {ECO:0000313|EMBL:EXI93170.1, ECO:0000313|Proteomes:UP000020878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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:EXI93170.1}.
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DR   EMBL; JEMZ01000001; EXI93170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011QVI3; -.
DR   STRING; 1454005.AW12_00026; -.
DR   PATRIC; fig|1454005.3.peg.26; -.
DR   Proteomes; UP000020878; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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:SF4; 1,6-ANHYDRO-N-ACETYLMURAMYL-L-ALANINE AMIDASE AMPD; 1.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EXI93170.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020878};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          26..174
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   193 AA;  21185 MW;  9A58A8CD4296D272 CRC64;
     MSWSRLPVAP AISDAGWLDG ALRIESANCD DRPAGETISL IVVHAISLPP ACFGGDAIMR
     LFTNRLDATA HPYFARIAGL RVSAHFLIRR DGELIQFVSC HQRSWHAGLS CWQGRPRCND
     FSLGIELEGC DELPFAEAQY ACLLPLLRFF CVHFPVTAVV GHSDIAPGRK TDPGPCFDWR
     RLASIGKLPG LLC
//
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