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Database: UniProt
Entry: E3BM23_9VIBR
LinkDB: E3BM23_9VIBR
Original site: E3BM23_9VIBR 
ID   E3BM23_9VIBR            Unreviewed;       209 AA.
AC   E3BM23;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=VIBC2010_01708 {ECO:0000313|EMBL:EFP95951.1};
OS   Vibrio caribbeanicus ATCC BAA-2122.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP95951.1, ECO:0000313|Proteomes:UP000002943};
RN   [1] {ECO:0000313|EMBL:EFP95951.1, ECO:0000313|Proteomes:UP000002943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP95951.1,
RC   ECO:0000313|Proteomes:UP000002943};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EFP95951.1}.
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DR   EMBL; AEIU01000083; EFP95951.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3BM23; -.
DR   STRING; 796620.VIBC2010_01708; -.
DR   eggNOG; COG3023; Bacteria.
DR   Proteomes; UP000002943; 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; 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:UP000002943};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          43..194
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   209 AA;  24256 MW;  F8AA4DC1B1AB0437 CRC64;
     MEIQPLISLF VIKKIKSKHI TQTMKRTMID ENGWYKDAKH VPSPFFDKRA SKKDISLLVI
     HNISLPPREY GGPYIEQLFM GKLNPKEHPF FKSIHKLKVS AHCLIKRGGD IVQFVSFYDR
     AWHAGESCFA KREKCNDYSI GIELEGDDAT AYTEEQYRSL ISLSRSIMIR YPEITPFRIT
     GHQYIAPLRK TDPGLSFDWP RFRSELTGT
//
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