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Database: UniProt
Entry: A0A1K1MSE5_9PROT
LinkDB: A0A1K1MSE5_9PROT
Original site: A0A1K1MSE5_9PROT 
ID   A0A1K1MSE5_9PROT        Unreviewed;       187 AA.
AC   A0A1K1MSE5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=SAMN05216414_10974 {ECO:0000313|EMBL:SFW26114.1};
OS   Nitrosovibrio sp. Nv17.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosovibrio.
OX   NCBI_TaxID=1855339 {ECO:0000313|EMBL:SFW26114.1, ECO:0000313|Proteomes:UP000183249};
RN   [1] {ECO:0000313|EMBL:SFW26114.1, ECO:0000313|Proteomes:UP000183249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nv17 {ECO:0000313|EMBL:SFW26114.1,
RC   ECO:0000313|Proteomes:UP000183249};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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   -!- 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; FPIQ01000009; SFW26114.1; -; Genomic_DNA.
DR   RefSeq; WP_072293834.1; NZ_FPIQ01000009.1.
DR   AlphaFoldDB; A0A1K1MSE5; -.
DR   OrthoDB; 9794842at2; -.
DR   Proteomes; UP000183249; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Reference proteome {ECO:0000313|Proteomes:UP000183249}.
FT   DOMAIN          22..170
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   187 AA;  20549 MW;  D352B56771DA20F9 CRC64;
     MSAGILHVGA AGWLRDVHRM PSPNHDERPD GCGVDLLVIH SISLPPDEFT GDDVIRLFMN
     TLDCASHPYY RRLHGLKVSA HFFIRRDGSL IQFVPCAKRA WHAGASCWRG RSGCNDFSVG
     IELEGSDSVP FADGQYGTLD GLTRALQQAY AIRDIVGHAD IAPGRKTDPG PHFDWMRYRA
     ALRAPGG
//
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