ID A0A0Q4MNR7_9GAMM Unreviewed; 568 AA.
AC A0A0Q4MNR7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ASF13_03575 {ECO:0000313|EMBL:KQN57885.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN57885.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN57885.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57885.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN57885.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57885.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:KQN57885.1}.
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DR EMBL; LMLK01000012; KQN57885.1; -; Genomic_DNA.
DR RefSeq; WP_056235397.1; NZ_LMLK01000012.1.
DR AlphaFoldDB; A0A0Q4MNR7; -.
DR STRING; 1736225.ASF13_03575; -.
DR Proteomes; UP000050856; 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; 2.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
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:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000050856};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..568
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006227286"
FT DOMAIN 452..495
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 522..565
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 128..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 60683 MW; 6ED164DE832F22D9 CRC64;
MRQVKSWLML ALLCCTFSTL AANLSDIQVA NGSNEATVKL SFAGQPVYAF FPLHNPERVV
LDIRQSGVVK GLPLEFSGEN LVKRIRSSEA KDSQSIRLVF ELTEAGKTRA VTQRNGSTYN
VVFTISSRQP AKPAARPAPV SSAGTSRPAP VSSEPAKNPF GANPVTTVTS GNQVARPRTS
RASSSDVAIV AIDAGHGGQD PGAIGPSGLK EKNVTIAIAR KLKELLNADP MFKGVMTRDG
DYFISVMGRS DVARKQNANL LVSIHADAAP SRSASGASVW VLSNRRANSE MAGWLEQHEK
QSELLGGAGD LLANSQADPY LSQAVLDLQF GHSQRVGYDV AVKVIAQLQR VGALHKRRPE
HASLGVLRSP DIPSLLVETG FISNPSEERL LGSSAYQQKI AESIYKGLRN YFLAHPLQSV
PKEENRPLQS AAAVNAEPEP APAGTVYTGA VQRHVVKRGE TLSGIAAQYG ASMATLRGMN
TLKKDVVWVG QRLKVPAGAQ TARVAKPVVT QAANRAKPKR AQRHKVVRGD SLTAIAVHYG
VSPQSIQQAN KMKSQNVMLG QTLTIPAS
//
