ID E6WU93_PSEUU Unreviewed; 539 AA.
AC E6WU93;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Psesu_1976 {ECO:0000313|EMBL:ADV27813.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27813.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV27813.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) 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};
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DR EMBL; CP002446; ADV27813.1; -; Genomic_DNA.
DR AlphaFoldDB; E6WU93; -.
DR STRING; 743721.Psesu_1976; -.
DR KEGG; psu:Psesu_1976; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_2_6; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000008632; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADV27813.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..539
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003215107"
FT DOMAIN 353..508
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 159..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 54064 MW; 34D51A872D5FC14F CRC64;
MCHLVARIGV LAAGLALAAA GCVGEALAGE IKGLSLQQGA TGTRAEVQLQ GAGEFKTMTL
AGPHRLVVDL PESHAAAGLK LPAPTGLVTG VRTGQPVPGT YRIVFELAEP VASLPVRTES
MPGGARLVIE WPGDGPARPA ATATAAARAT AAAGAATGAA TAPATTSPVP ATATASNTAA
SDADARAEAA RATALLTAQV VQAGRANPPA AQAVVPAAST PGSTTATAPA APGVSPQAIL
EGRAGASVAS APSPASTSPA TPATATPDTE SVAAAPAPVR ALPNASSARP LVVAIDAGHG
GQDPGAVGPT GKREKDVTLA MARELARQVN ATPGLKAFLV RDSDVFIPLP MRAQRARAAK
ADIFISIHAD AAENRNARGS SVYVLSTKGA SSQRARWLAD KENAADLVGG VRLQQTEAVL
ANVLLDLAQS GHMRASEDAA VHVLGGLKRV GNNHKPNIER ANFAVLRTSD MPAMLVETAF
ISNAEEEARL VDPSFQRKVA GAVLDGITTY FSRQPPPGTL FAMRAEADLV AASGTGGTP
//
