ID A0A0G3CVC0_9GAMM Unreviewed; 283 AA.
AC A0A0G3CVC0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=QQ39_11615 {ECO:0000313|EMBL:AKJ43873.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ43873.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ43873.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ43873.1,
RC ECO:0000313|Proteomes:UP000068021};
RX PubMed=26159528;
RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT Bacterium from the Family Enterobacteriaceae.";
RL Genome Announc. 3:e00740-15(2015).
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; CP010423; AKJ43873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3CVC0; -.
DR STRING; 82985.QQ39_11615; -.
DR KEGG; pfq:QQ39_11615; -.
DR PATRIC; fig|82985.3.peg.2435; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000068021; Chromosome.
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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
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 PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF10; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000068021}.
FT DOMAIN 40..185
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 283 AA; 32408 MW; 0F8B93A593550AD5 CRC64;
MIGIILKQVK FFFQACFCLL VLTCSGCSNL RDAGDYWVDE SHVALGQESR VQFLVFHYTA
ENDENSLRIL SGNNVSVHYL INHQPEQMSG RPVVLQLVPE AQRAWHAGAS FWRGRNNLND
TSIGVEIVNA GYHKVGNKRS WEPYNERQID LLIALSWDII QRHHIDPANV VGHSDIAPQR
KIDPGPLFPW DRLAQVGIGA WPDVGRVQYY QRLREAETSI DIAELQANLK KYGYKVPETG
QLDDETRRVI KAFQMHFRQD KYSGHPDAET LAILDALLEK YRR
//
