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Database: UniProt
Entry: W4ARV1_9BACL
LinkDB: W4ARV1_9BACL
Original site: W4ARV1_9BACL 
ID   W4ARV1_9BACL            Unreviewed;       469 AA.
AC   W4ARV1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ETT34230.1};
GN   ORFNames=C161_18745 {ECO:0000313|EMBL:ETT34230.1};
OS   Paenibacillus sp. FSL R5-192.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT34230.1, ECO:0000313|Proteomes:UP000019041};
RN   [1] {ECO:0000313|EMBL:ETT34230.1, ECO:0000313|Proteomes:UP000019041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT34230.1,
RC   ECO:0000313|Proteomes:UP000019041};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT34230.1}.
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DR   EMBL; ASPR01000024; ETT34230.1; -; Genomic_DNA.
DR   RefSeq; WP_036671959.1; NZ_ASPR01000024.1.
DR   AlphaFoldDB; W4ARV1; -.
DR   PATRIC; fig|1226754.4.peg.3806; -.
DR   Proteomes; UP000019041; 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..469
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004838101"
FT   DOMAIN          356..463
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          140..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  50066 MW;  4D63DB492E73A596 CRC64;
     MKKFGFLVLL FVFGLVFPGY SHAATDTKII LDGKEIVQPS DTKAEIINSK VMVPIRVVSE
     NLGYSVEWKQ QTQTVTISKD NTAMQMIVGQ KTATVNGSNV NLDAPPLVKN GTTLVPLRFI
     GEEMGLKVGW NNTTKTVTLV TQNSGSGNGT TTPPNSGNEG GGSDQEGLVL VNGISFSDNR
     FMIATSGSTK PNVFTMTGPD RIVIDLPNTA FADSFSEGQA LDSNQNGQLV VSGYPDVSKI
     RYSLYSNSPS TIRFVIDLSS SKGYSVQNDS GLVMINLDNQ SGTPAPPVGN NGKKVVVIDA
     GHGDQDPGAI GVTGKREKDF NLAMALKVEA LLKKESKIDV VLTRSDDTFL ALKERVKIAQ
     DIKADIFISI HANSGPAAAN GVETFYTRSN SKALATVMHK YLLQSSGLKD RGVKTASLHV
     TRETTMPAVL LEGGFLSNKS DEAALFTESF QKSVAKGIVA GIKEYLGIK
//
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