ID A0A0S2DNC8_LYSEN Unreviewed; 660 AA.
AC A0A0S2DNC8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=GLE_4707 {ECO:0000313|EMBL:ALN60048.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN60048.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN60048.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN60048.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) 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}.
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; CP013140; ALN60048.1; -; Genomic_DNA.
DR RefSeq; WP_057949251.1; NZ_CP013140.1.
DR AlphaFoldDB; A0A0S2DNC8; -.
DR STRING; 69.GLE_4707; -.
DR KEGG; lez:GLE_4707; -.
DR PATRIC; fig|69.6.peg.4641; -.
DR Proteomes; UP000061569; Chromosome.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000061569};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..48
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 49..660
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006595505"
FT DOMAIN 321..464
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 660 AA; 70600 MW; F117F6D631C7BB75 CRC64;
MNEYSVTRRA RRRPLSRAFC SRILSAKPLS CLSLALSLAC GFIVDAHAAE RANAAPQDPA
LAQRLRLEES LSRIDRQLYA GYFRQAYARY PSIPAGTLEA VAYVTTRWQH LQPDGAGYGE
QHQHMPRAYG VMGLYHGEGF ADQVGEGARL LGVPAQRVMR DPASNILAAA ALLDRELRAD
AVSAKSPVEA TRAALERYAG FAPAGAGAAA KSAVQAHARA SFAFDVLSAQ DKGVNDRGIV
VPARAVAWER AFDAPALLRL RAPFVRLDVA ADKVEALGAD EGGWRIDPLD ETLRAPAGSR
SEVAAAAEKS TDYPPALWVA SPYHSARTSY DSVTIHTMQG YYAGSISWFQ NNPNSVSAHY
LIRSSDGQIT QMVRENRAAH HVGVHNKTTL GIEHEGFIAN ASWYTAAMYN ASAALTRHFC
ATYSAISCAS AFKGPGGTGI NVLPASVKVK GHQHYSSQTH TDPGQYWDWA RYYNLLNPGT
PGGGSVIDSF ESSVGHFDSA PAYSGSTTGI SAASLAERNC TTRKNGECSL RVLLKDDAAS
ANAWAVRLLS GGGNPGSNAA LTRAGGKVGV WVYTGASGLS AAVGIDDSDG TERSVARAIP
VNTWTYLEWR LDDAAQWDAW VGGANGAITA ATVKLDAVWL YRDQTSFDVN VYLDDVQVKN
//
