ID S0A0S6_9CAUD Unreviewed; 138 AA.
AC S0A0S6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=Phi46:1_gp12 {ECO:0000313|EMBL:AGO47823.1};
OS Cellulophaga phage phi46:1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=1327974 {ECO:0000313|EMBL:AGO47823.1, ECO:0000313|Proteomes:UP000014718};
RN [1] {ECO:0000313|EMBL:AGO47823.1, ECO:0000313|Proteomes:UP000014718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phi46:1 {ECO:0000313|EMBL:AGO47823.1};
RX PubMed=23858439; DOI=10.1073/pnas.1305956110;
RA Holmfeldt K., Solonenko N., Shah M., Corrier K., Riemann L.,
RA Verberkmoes N.C., Sullivan M.B.;
RT "Twelve previously unknown phage genera are ubiquitous in global oceans.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:12798-12803(2013).
RN [2] {ECO:0000313|Proteomes:UP000014718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Holmfeldt K., Solonenko N., Shah M., Corrier K., Riemann L.,
RA VerBerkmoes N.C., Sullivan M.B.;
RT "The Cellulophaga phages: a novel, diverse, and globally ubiquitous model
RT system.";
RL Submitted (MAR-2013) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; KC821611; AGO47823.1; -; Genomic_DNA.
DR RefSeq; YP_008241819.1; NC_021800.1.
DR GeneID; 16796655; -.
DR KEGG; vg:16796655; -.
DR OrthoDB; 13080at10239; -.
DR Proteomes; UP000014718; 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:UP000014718}.
FT DOMAIN 1..126
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 138 AA; 15831 MW; 21E99CBD03F4E9E9 CRC64;
MRTIKYIVLH CTATVQHAKV ENIIKYWRNV LKWKSNGYHF IIESSGKVHN ITPIENVANG
VAGYNSASIH ISYIGGIDKN GKALDNRTPE QIEAQKQLIR TLTKQFPNAE IKGHRDFPNV
RKDCPSFDVK SWLKTWLK
//
