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Database: UniProt
Entry: A0A1M7YHP0_9FIRM
LinkDB: A0A1M7YHP0_9FIRM
Original site: A0A1M7YHP0_9FIRM 
ID   A0A1M7YHP0_9FIRM        Unreviewed;       229 AA.
AC   A0A1M7YHP0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SAMN02745217_03508 {ECO:0000313|EMBL:SHO52106.1};
OS   Anaerocolumna xylanovorans DSM 12503.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerocolumna.
OX   NCBI_TaxID=1121345 {ECO:0000313|EMBL:SHO52106.1, ECO:0000313|Proteomes:UP000184612};
RN   [1] {ECO:0000313|EMBL:SHO52106.1, ECO:0000313|Proteomes:UP000184612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12503 {ECO:0000313|EMBL:SHO52106.1,
RC   ECO:0000313|Proteomes:UP000184612};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-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};
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DR   EMBL; FRFD01000010; SHO52106.1; -; Genomic_DNA.
DR   RefSeq; WP_073590149.1; NZ_FRFD01000010.1.
DR   AlphaFoldDB; A0A1M7YHP0; -.
DR   STRING; 1121345.SAMN02745217_03508; -.
DR   OrthoDB; 9794294at2; -.
DR   Proteomes; UP000184612; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; 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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184612};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..199
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   229 AA;  26222 MW;  4C74BC5FCBCFDE19 CRC64;
     MNVKNRRRRR KRRSRLFRLT TVTSLCMLMA VIIGIMLLSA IKHFREGSYG FAYYTIAPPP
     ITENLLTPNP YSRSEEPLKK VKGIVIHYTA NPGTSAEANR NYFENLKSQR ETSASSHFII
     GLEGEILQCI PLDEISFASN DRNVDTISIE CCHPDATGKF NEKTYASLVA LSAWLCSKYR
     LDEKDILRHY DITGKLCPLY YVKHEDAWNT LKENIFTYLK EKEASAELG
//
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