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Database: UniProt
Entry: A0A257TU18_9BACT
LinkDB: A0A257TU18_9BACT
Original site: A0A257TU18_9BACT 
ID   A0A257TU18_9BACT        Unreviewed;       187 AA.
AC   A0A257TU18;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=B7Z63_01160 {ECO:0000313|EMBL:OYV88141.1};
OS   Ignavibacteriae bacterium 37-53-5.
OC   Bacteria; Ignavibacteriota.
OX   NCBI_TaxID=1970532 {ECO:0000313|EMBL:OYV88141.1, ECO:0000313|Proteomes:UP000225652};
RN   [1] {ECO:0000313|EMBL:OYV88141.1, ECO:0000313|Proteomes:UP000225652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37-53-5 {ECO:0000313|EMBL:OYV88141.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-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:OYV88141.1}.
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DR   EMBL; NCBO01000053; OYV88141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257TU18; -.
DR   Proteomes; UP000225652; 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; 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; 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          37..172
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   187 AA;  21081 MW;  1240D0C8A9631790 CRC64;
     MSYTLLIGFL LFLGQPQMSP TQAPCAHVKI IDRLVQWGHK DANHPRKIEA IIIHSSYNAL
     TPDSFSIAGI LQEYKNIGVS PHYIIDRNGA IYRLVRDRDI AYHAGKSRLP DGKTNVNAVS
     IGIEIVNTIH DSPTDAQYIS LAELVKCLEG KYNIKYVLGH SDIAPGRKTD PWNFDWKKFD
     RLLKGQK
//
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