ID C1D367_DEIDV Unreviewed; 359 AA.
AC C1D367;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Deide_2p01860 {ECO:0000313|EMBL:ACO47856.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide2 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47856.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47856.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RC PLASMID=pDeide2 {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR EMBL; CP001116; ACO47856.1; -; Genomic_DNA.
DR RefSeq; WP_012695326.1; NC_012529.1.
DR AlphaFoldDB; C1D367; -.
DR KEGG; ddr:Deide_2p01860; -.
DR HOGENOM; CLU_752032_0_0_0; -.
DR OrthoDB; 9812621at2; -.
DR Proteomes; UP000002208; Plasmid pDeide2.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01471; PG_binding_1; 2.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ACO47856.1};
KW Hydrolase {ECO:0000313|EMBL:ACO47856.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Plasmid {ECO:0000313|EMBL:ACO47856.1};
KW Protease {ECO:0000313|EMBL:ACO47856.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..359
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002905937"
FT DOMAIN 46..199
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 58..205
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 359 AA; 37982 MW; A6A1064F3378A97B CRC64;
MNTLLTRRDL LRWGALLGGS TLLASCGLQA PPMADLPLNT QAVTAPSISS TSTWKAQAPR
EAITLLSARP TRIIVHHTAS ANVTDYSQAQ AFTLARSIQQ SHFDRGWIDS GQQFTISRGG
YVVEGRHRSL EAAQGGTHHV RGAHCDGFND VAVGIENEGT YMTVSPPAGQ YSALVSLCAW
LCQHYGIPAT ELYGHRDFNT TACPGDLLYG QLPQLRRDVA TRLGVTVRIW PTTRSGQTGE
RVRSAQRLLV SHGQSLTADG SYGPATASAV SAFQSGAGLT PDGVIGSATW ERLIRTVRRG
DSGPAVQAAQ GQLAARGYGV TADGVFGAGT ESAVRSFQSS RGLTSDGIVG PNTWHALES
//