ID D4P7C1_9CAUD Unreviewed; 265 AA.
AC D4P7C1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=Pepy6gene010 {ECO:0000313|EMBL:ADD80901.1};
OS Rhodococcus phage ReqiPepy6.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Pepyhexavirus; Pepyhexavirus pepy6.
OX NCBI_TaxID=691965 {ECO:0000313|EMBL:ADD80901.1, ECO:0000313|Proteomes:UP000002347};
RN [1] {ECO:0000313|EMBL:ADD80901.1, ECO:0000313|Proteomes:UP000002347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097585; DOI=10.1128/AEM.01952-10;
RA Summer E.J., Liu M., Gill J.J., Grant M., Chan-Cortes T.N., Ferguson L.,
RA Janes C., Lange K., Bertoli M., Moore C., Orchard R.C., Cohen N., Young R.;
RT "Genomic and functional analyses of Rhodococcus equi phages ReqiPepy6,
RT ReqiPoco6, ReqiPine5, and ReqiDocB7.";
RL Appl. Environ. Microbiol. 77:669-683(2011).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU580941; ADD80901.1; -; Genomic_DNA.
DR RefSeq; YP_009017624.1; NC_023735.1.
DR GeneID; 18565587; -.
DR KEGG; vg:18565587; -.
DR OrthoDB; 2745at10239; -.
DR Proteomes; UP000002347; Genome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
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 Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000002347}.
FT DOMAIN 16..151
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 265 AA; 29326 MW; 7A7624B89257CD61 CRC64;
MDVLRAFGVK VKEFDAWRDR GQGDFFTIWG VIAHHTGSNN ASAASIAYGH EGLKGLLSQI
HLDRNGVATI TGAGIAWHAG VGSWPGIQTN NANAVTIGVE ANSDGVSPWP PEMLDAYHRI
CAAICWFLGH SSLRTIGHKE WAKVQGKWDP GGIDMAQFRA KVQYYIDHPP FMPPPQPVTE
AGEPMAFWDD QVPTILSPEK SFPRHEYLQL IDMHAFLANT QSKQVLDQMK LVRDDNQRIL
NEMQLMRDDL SELATAVLSG VKKDG
//
