ID A0A1Z9WPB1_9GAMM Unreviewed; 441 AA.
AC A0A1Z9WPB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=CBC19_02290 {ECO:0000313|EMBL:OUX79569.1};
OS Oceanospirillales bacterium TMED59.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX NCBI_TaxID=1986765 {ECO:0000313|EMBL:OUX79569.1, ECO:0000313|Proteomes:UP000195499};
RN [1] {ECO:0000313|EMBL:OUX79569.1, ECO:0000313|Proteomes:UP000195499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED59 {ECO:0000313|EMBL:OUX79569.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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:OUX79569.1}.
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DR EMBL; NHDM01000027; OUX79569.1; -; Genomic_DNA.
DR Proteomes; UP000195499; 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; cd00118; LysM; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
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 Pfam; PF01476; LysM; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..441
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012916478"
FT DOMAIN 393..436
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 441 AA; 48771 MW; 14C23547249DF735 CRC64;
MIRFFITXIA CLXAPFAQAV DLQSVRSSAD QDSSRVVLEF SGKPQFSHFN LNNPSRLVLD
IRNLTAKTLS PLDSIDDSRI QRIRSSIRGN GRRLVFDLSG EYRSHVFTLG PKGPYPHRLV
VDVVGYVAGE KASSRSAXPN ETAEPLVEKR DIVVAIDPGH GGKDPGASSY GVVEKQXVLQ
IAKRLAKRFQ SEPGYRAVLT REXDRYIPLK DRPRIAREAG ADFFISIHAD SFPKNRNVRG
TGVYALSLRG ANSELSRWLQ NTENADDLAG GVDLGDVDND TRQVLLNMSM ESAIRISKQA
GEGVXSDLKD AGRVHKKRLG LANFVVLRSP DIPSLLIETG FLSNRSDAKR LSISREQEKI
AAAIFEGIKR YFEKSPPANT FVAWRKQNAD QRMIIEVKRG DTLSEIAARY GLSLQALKEL
NGLETNVIHL GQKLEVPGSS R
//
