ID A0A160MZ74_9GAMM Unreviewed; 486 AA.
AC A0A160MZ74;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ATSB10_12290 {ECO:0000313|EMBL:AND68683.1};
OS Dyella thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=445710 {ECO:0000313|EMBL:AND68683.1, ECO:0000313|Proteomes:UP000077255};
RN [1] {ECO:0000313|EMBL:AND68683.1, ECO:0000313|Proteomes:UP000077255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATSB10 {ECO:0000313|EMBL:AND68683.1,
RC ECO:0000313|Proteomes:UP000077255};
RA Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA Madhaiyan M.;
RT "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL Submitted (FEB-2016) 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; CP014841; AND68683.1; -; Genomic_DNA.
DR RefSeq; WP_063671264.1; NZ_CP014841.1.
DR AlphaFoldDB; A0A160MZ74; -.
DR STRING; 445710.ATSB10_12290; -.
DR KEGG; dtx:ATSB10_12290; -.
DR PATRIC; fig|445710.3.peg.1229; -.
DR Proteomes; UP000077255; 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; cd00118; LysM; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
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:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AND68683.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077255};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..486
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007817876"
FT DOMAIN 438..483
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 486 AA; 51582 MW; 877EA0E3E5C06F99 CRC64;
MRASLFRFGL CALVAAAAGL SSPVRAAEIR GARVWAGPEY TRVVFDLSGP VRYDITPRGD
QIRVDLGNDR LASAFEKPTA QGLFKGVTAH RRGGKLELLA DVSAGTTPKS FMLKPGGGYG
YRLVLDLYPK SVAKAPDAKA SAPATRVAKA TVTKADKREV LTLRQVAEQM GGERKVVVAV
DAGHGGVDPG AHGPHGTLEK NVTLAVARKL AALIDKQPGM QAVLTRDGDY FIPLKRRYEI
AREKNADLFV SIHADAFRNG DAKGSSVWVL SSRGKSTVAA RWLADRENSS DLIGGVSLAS
EDDSLASVLL DMQQGWAVQA SESIAGNVLK ALGKLGPTHR GYVERANFVV LRSPDVPSIL
VETAFISNPS EERKLRDPEH QTELAEAVMG GVRNYFETTP PPGTWFAAQA ARRNGTLLAS
TQAIDAPAGK RADDSVQDMH KVARGESLGS IARQYGVSVG ALKSANRISG NGDTLRAGSV
LTIPAS
//
