ID A0A0M1J547_9GAMM Unreviewed; 391 AA.
AC A0A0M1J547;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE Flags: Fragment;
GN ORFNames=TI04_12085 {ECO:0000313|EMBL:KOR27977.1};
OS Achromatium sp. WMS2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604835 {ECO:0000313|EMBL:KOR27977.1, ECO:0000313|Proteomes:UP000037003};
RN [1] {ECO:0000313|EMBL:KOR27977.1, ECO:0000313|Proteomes:UP000037003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS2 {ECO:0000313|EMBL:KOR27977.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
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:KOR27977.1}.
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DR EMBL; JXSN01000489; KOR27977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1J547; -.
DR Proteomes; UP000037003; 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; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000037003};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..391
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005617576"
FT DOMAIN 294..391
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 140..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 391
FT /evidence="ECO:0000313|EMBL:KOR27977.1"
SQ SEQUENCE 391 AA; 42021 MW; FAE0C1FFD425239E CRC64;
MKKNIFIVGL ALLALSAAAS AVQPIVKDIS FQQVGDSVRL VIGMTQNVEP KISYLVDPDR
MVIDVSGAVL KSNPPTIPPA ASSFIKAVRG GYFDPTTVRI VIDFDDRTMA RDHWLSPDSN
TGYKFTIDFK STARVLPQPR AAERYSSAPR PPAVRPSAPR QPQPAAYSPI VDRSQNVATP
VYTNNNGYAP NSANNGYAAR PQRDYYGTDY ARPAVRDVFA NGQLNSQPGR DLIIAIDPGH
GGKDTGAVGL NGTCEKDVVL SIGRRLAMQI NSTPGMRAVL TRSDDIFIPL RERVAIARSA
RADLFISIHA DAAYNRAAQG ASVYTLSERG ASSEAAKLLA NKENAADLVG GVSYSGDDLL
TITLLDMSLS ATMEASRNVA EHVLDRLYQV G
//
