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Database: UniProt
Entry: A0A1U9N961_9GAMM
LinkDB: A0A1U9N961_9GAMM
Original site: A0A1U9N961_9GAMM 
ID   A0A1U9N961_9GAMM        Unreviewed;       180 AA.
AC   A0A1U9N961;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=B0D95_08740 {ECO:0000313|EMBL:AQT60171.1};
OS   Cellvibrio sp. PSBB023.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT60171.1, ECO:0000313|Proteomes:UP000189646};
RN   [1] {ECO:0000313|EMBL:AQT60171.1, ECO:0000313|Proteomes:UP000189646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSBB023 {ECO:0000313|EMBL:AQT60171.1,
RC   ECO:0000313|Proteomes:UP000189646};
RA   Peterson S.W.;
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   -!- 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}.
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DR   EMBL; CP019799; AQT60171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9N961; -.
DR   STRING; 1945512.B0D95_08740; -.
DR   KEGG; ceb:B0D95_08740; -.
DR   OrthoDB; 9794842at2; -.
DR   Proteomes; UP000189646; Chromosome.
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; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189646};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          16..167
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   180 AA;  20004 MW;  42CA91FECD531C9E CRC64;
     MMIHDGWLSG VNICPSPNSN SRPESVDISL LVVHNISLPP GEFGGGYVQA FFQNRLDINA
     HPYFETIAGL QVSAHLFIER DGAITQFVPF TARAWHAGAS SFDGVSNCND YSVGVELEGT
     DELPYTDAQY LALEKVTRQL MLTYPKLTLE RITGHEHIAP GRKTDPGPAF DWQRFRRALL
//
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