ID A0A1J5M1N1_9PROT Unreviewed; 413 AA.
AC A0A1J5M1N1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=BM562_01285 {ECO:0000313|EMBL:OIQ33673.1};
OS Alphaproteobacteria bacterium MedPE-SWcel.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ33673.1, ECO:0000313|Proteomes:UP000183546};
RN [1] {ECO:0000313|EMBL:OIQ33673.1, ECO:0000313|Proteomes:UP000183546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ33673.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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:OIQ33673.1}.
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DR EMBL; MPDC01000001; OIQ33673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5M1N1; -.
DR STRING; 1860092.BM562_01285; -.
DR Proteomes; UP000183546; 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:0000256|ARBA:ARBA00022801}.
FT DOMAIN 243..398
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 413 AA; 44816 MW; F02120F77E835A9F CRC64;
MRRLLLALPV ILAALWLMVL PFPASAQGFT ALARVMPQDS RLIADGRGGV QLDLHLSQGV
PYRIFTLDAP RRLVLDFQEV DWTGLDPQAF LAPPQMRNIR FGGYLPGWSR MVLELAEPME
VATASMSIDT VSAAAALTVQ LQPTDAESFA AAAGAPHDPR LDLPPPAVLQ DRPARDPDAP
LVVMLDPGHG GLDPGAEAEG GVMEKELMLN FAYDLGERLV RSGAFEVLLT REGDYFVSLE
RRIAMAHQQG ADLFLSLHAD SVSEGMAHGT VVYTLSKEAS DLASVKLAER HDRADLLSGS
DLSTVDDEVT DVLLDLARQE THPRSTALAQ SVIEALMEQG GPVNRRPLRA AGFSVLKSAD
IPSILIELGF MSSPRDLENL TNPAWRAKAA QAILEGLMAW REDDTARRAL VRQ
//