ID A4XPY4_PSEMY Unreviewed; 471 AA.
AC A4XPY4;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Pmen_0632 {ECO:0000313|EMBL:ABP83400.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP83400.1};
RN [1] {ECO:0000313|EMBL:ABP83400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP83400.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP83400.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XPY4; -.
DR STRING; 399739.Pmen_0632; -.
DR KEGG; pmy:Pmen_0632; -.
DR PATRIC; fig|399739.8.peg.639; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_014322_2_3_6; -.
DR OrthoDB; 9806267at2; -.
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; IPR021731; AMIN_dom.
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; PF11741; AMIN; 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:ABP83400.1}.
FT DOMAIN 420..463
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 136..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 50060 MW; FAA1E4B5FECDE6C0 CRC64;
MRIGALVTAV GVLWAALAAE VLAASDVRGV RLWRAPDNTR LVFDLSGPVQ HSVFTLAAPD
RIVIDVSGAK LATNLEQLSL ANTPITGVRS AQRSADDLRV VIDLSAPVTP KSFSLAPNQQ
YGHRLVVDLF DQGSTPPAAQ TPSVAASAPP VPVTPTQPPP KLTPVPNGKR DIIIAIDAGH
GGEDPGALSP VKGQYEKHVT LAISRELQRQ INAEKGFRAE LVRTGDYFIP LRKRTEIARK
KGADLFVSIH ADAAPRASAF GASVYALSER GATSETARWL ADAENQSDLI GGAGNVSLDD
KDKMLAGVLL DLSMTASLSS SLNVGQKVLS NMGRITPLHK RRVEQAGFMV LKSPDIPSIL
VETGFISNPN EAKKLHTASH QQALARSITS GVKQFFHENP PPGTYVAWLR DEGKIAAGPR
EHVVARGESL ALIAQRYQIS LAVLRSANNL NGDVIKVGQT LQIPATALAA Q
//
