ID A0A0Q9R6Y3_9BACL Unreviewed; 478 AA.
AC A0A0Q9R6Y3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN ORFNames=ASG93_17510 {ECO:0000313|EMBL:KRF10731.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF10731.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF10731.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF10731.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF10731.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF10731.1,
RC ECO:0000313|Proteomes:UP000051948};
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 -!- 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:KRF10731.1}.
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DR EMBL; LMSP01000047; KRF10731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9R6Y3; -.
DR STRING; 1736411.ASG93_17510; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_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; PF07833; Cu_amine_oxidN1; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..478
FT /note="MurNAc-LAA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006382313"
FT DOMAIN 365..472
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 144..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 52516 MW; CDCB1C9DF8909359 CRC64;
MKFPAFYIML LVCMLLLPSY AMGAESTSGI KLYMNEKKLV SNEVQPRIVN GNTIVPVRII
VEEIGAKVSW DEPTRKVTIV KDDMNIQLVI DSKTALIKGK KENLEVAPII EKGNTMLPLR
FIGQLMGIEF KWDSLTSSVH MFKKDDSDSK PVTGPIDVVE DPNHGEVTPP KPSVPGTGTD
PGTIKPDPNA HLLTSIVLSE KELTVTAKDG SLVPTMMKLS NPNRIVFDFP NTSLDPSLQK
LLVNNAGELP SKHPLVEKVR FSNFSDNPAT VRIILDLKGS ADYRIQPSKN PNQWSAAIVE
HQLTVVIDAG HGDNDPGALS ITGKHEKDFT LATAKKVEKL LVQDKRVNVL MTRSDDTFIP
LDGRVSFAND IQTDLFLSIH GNSANATVSG TETYYNRPES LAFANVIHKN VVAAAGLPDR
KVRQADFRVI TKTTMPAVLV EVGYLSNKND ESAMFKEAFQ DKVAASIVAA FKEYLNLK
//
