ID A0A0D0S3F7_9GAMM Unreviewed; 645 AA.
AC A0A0D0S3F7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=TI01_2267 {ECO:0000313|EMBL:KIQ96185.1};
OS Lysobacter sp. A03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1199154 {ECO:0000313|EMBL:KIQ96185.1, ECO:0000313|Proteomes:UP000032077};
RN [1] {ECO:0000313|EMBL:KIQ96185.1, ECO:0000313|Proteomes:UP000032077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A03 {ECO:0000313|EMBL:KIQ96185.1,
RC ECO:0000313|Proteomes:UP000032077};
RA Pereira J.Q., Ambrosini A., Sant'Anna F.H., Tadra-Sfeir M., Faoro H.,
RA Pedrosa F.O., de Souza E.M., Brandelli A., Passaglia L.M.;
RT "Genome sequence of Lysobacter sp. A03.";
RL Submitted (JAN-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIQ96185.1}.
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DR EMBL; JXSS01000103; KIQ96185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0S3F7; -.
DR STRING; 1199154.TI01_2267; -.
DR PATRIC; fig|1199154.3.peg.522; -.
DR Proteomes; UP000032077; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KIQ96185.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032077};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..645
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002220974"
FT DOMAIN 305..450
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 645 AA; 68986 MW; EDEA1462F05A3B4D CRC64;
MLSVAISGLL ASTAFAGEST ALPEEAALVE QLNVEEAALR PQRLAFQRYF KEAYALYPAV
PVGTLEAVAY VQSRWLNIQP DANESQTEAH HHMPAAYGVM GLYAGQGFAD QVTAGAQLLG
VSPALVRTDA RTNVLAAAAL LDAEIRKDHP AADSRTRLKR GGNTPSPEEI RPALMRYAGF
SASPVEAARA SAVGEYARTS FAYDVLLAQD RGVNDRGIVV PERAIEWERA FDMDQLITQR
APMVRLDVAN DRIETADYEI DPISETLRAK SAETRPTVKG AAAAGPDAGI QSTDYGPAIW
NAAHSSNYNA SRSAAVSAVA IHTAQGSYAG TISWFKNSSS NVSAHYVIRS SDGQVTQMVR
NAHTAWHLRN QNSFALGIEH EGYVNNSSWY TNAMYNASAG VVRSFCAKYS TIPCSSAYKG
APSSGINVLP TSVKIKGHQH YSGQTHTDPG INWNWSKYYG LLNPGSGGTV KYLDRFESSV
GHFNTSPAYS GSTTGISSAS TATRDCSTRK NGSCSLRVLL KDNKSSSANW AVRLLSGSGN
PGSNTALTRA NGTVGFWVWS GGTGTSVGVG IDDSDGTERS TSKSVPANKW TYVSWSLPTS
SNWNAWVGGN GAISASTVKM DAIWLYHANT AYDVNVYIDD VQIKN
//
