ID C6AUW1_RHILS Unreviewed; 442 AA.
AC C6AUW1;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Rleg_1394 {ECO:0000313|EMBL:ACS55686.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS55686.1, ECO:0000313|Proteomes:UP000002256};
RN [1] {ECO:0000313|EMBL:ACS55686.1, ECO:0000313|Proteomes:UP000002256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS55686.1,
RC ECO:0000313|Proteomes:UP000002256};
RX PubMed=21304718;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain
RT WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS55686.1; -; Genomic_DNA.
DR AlphaFoldDB; C6AUW1; -.
DR KEGG; rlg:Rleg_1394; -.
DR HOGENOM; CLU_014322_2_1_5; -.
DR Proteomes; UP000002256; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACS55686.1}.
FT DOMAIN 277..431
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 442 AA; 47812 MW; E6C3E1599845D8D1 CRC64;
MFRHRDVGRS RVGSIAIQIG CGGLLFKRAR IAAKSAARRS TFARRVLAAL LVVSLLPAAA
SSVEAKDPLL AYGARIVGDD ARTRIVIDFD REPRFSVHYI ANPERIVVDL PATAFGFAAK
DLAARGLFKD IRYGKMDEES ARIVLTTTGP VKLALAKVQA DETGNGHRLV LDAEMIDKKA
FAELVKTQSW SDRTEAAQTT SAIPAPQKAA PGDFVIAVDA GHGGIDTGAI GVDTKTEEKQ
VTLAFAKALT DRLNKEPGIK AFLTREDDEF LSLSQRVLIA RQNHAGLFIS LHADTLKQKD
IRGATVYTIS DKASDKLAAD LAERENLSDQ IAGKETVAEP PEVADILLDL TRRETQAFSI
SLAESVLNSF KDQVGTINNP HRHAGFRVLQ APDVPSILLE IGFLSNAEDE KLLLDEAWRG
KIAGLLTDAV KRYRAAVMAN GG
//
