ID A0A0D6SYR0_9PSED Unreviewed; 396 AA.
AC A0A0D6SYR0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SZ55_1403 {ECO:0000313|EMBL:KIV73463.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV73463.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV73463.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV73463.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
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 -!- 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:KIV73463.1}.
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DR EMBL; JYFT01000020; KIV73463.1; -; Genomic_DNA.
DR RefSeq; WP_044403459.1; NZ_JYFT01000020.1.
DR AlphaFoldDB; A0A0D6SYR0; -.
DR PATRIC; fig|1604022.3.peg.4477; -.
DR Proteomes; UP000032531; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KIV73463.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..396
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002313458"
FT DOMAIN 216..374
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 396 AA; 42348 MW; 7C8895EEA489856E CRC64;
MDRRHLLKFV LAGFTLPFAS TASAAQAVTQ VRSWRTADRL RIVLDLSGPV NFRSFALAAP
ERVIVDLDDT RLLAQLQDLA LGQGPIRSVR SGLQGRSTRL VFDLQAPAQL SSFLLPPGEG
KGHRLVLDFQ PLTPTPALAP AAPAVAPAGG QRDIVVAIDA GHGGKDPGAI GFNGEQEKAV
ALAIARLLAR KVNAQKGFRA HLVRNDDVFV PLRKRVEIAR RRNADLFISV HADAAPRRSA
SGASVFALSQ GGATSTTARW LAERENRVDL IGAERLLSLK DKDPMLAGVI LDMSMTATIA
TSLDLGKSIL GSLQGVAGVH QKRVEQAGFA VLKSPDIPSV LVETGFMSNP GDCRRLIDAR
HQQRVANAIF DGLHRHFRAA PPQGTLLASM KASQNS
//
