ID F5Y3P0_RAMTT Unreviewed; 440 AA.
AC F5Y3P0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiC {ECO:0000313|EMBL:AEG93697.1};
GN OrderedLocusNames=Rta_25960 {ECO:0000313|EMBL:AEG93697.1};
OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS TTB310).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG93697.1, ECO:0000313|Proteomes:UP000008385};
RN [1] {ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA Barras F., Heulin T.;
RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG93697.1, ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RX PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA Vermeglio A., Achouak W., Heulin T.;
RT "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL PLoS ONE 6:E23784-E23784(2011).
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; CP000245; AEG93697.1; -; Genomic_DNA.
DR RefSeq; WP_013901929.1; NC_015677.1.
DR AlphaFoldDB; F5Y3P0; -.
DR STRING; 365046.Rta_25960; -.
DR KEGG; rta:Rta_25960; -.
DR PATRIC; fig|365046.3.peg.2653; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_2_4; -.
DR Proteomes; UP000008385; 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 Reference proteome {ECO:0000313|Proteomes:UP000008385}.
FT DOMAIN 270..425
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 178..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 47273 MW; A11F2E70F2640619 CRC64;
MTLSRRELLH GGALVLLLGA HQIARGASIM AVRIWPAPDY SRVTIESDGK LRSRQIVVTS
PPRLAVDIEG IELNPALREL VAQVQADDPY IAGIRVGQFS PDVVRLVIDL KQAALPQVFN
LPPVAAYQHR LVLDFYPQQP VDPLETLIAQ QMKENAWGSA PPSGTVADPL DELIARQGQR
PPTAGTGRSG GSKPSGGDKT DRLIIIALDP GHGGEDPGAI GPGGTREKDV VLQVAQRLQA
RINASSVGGN PMRAFLTRDA DFFVPLQVRV QKARRVQADL FVSIHADAFI TPSARGASVF
ALSHNGASST AARWLADKEN RADLIGGLNV KSQDAQVARA LLDMSTTAQI NDSLKLGHAM
LGEIGNVGRL HKPRVEQAGF AVLKAPDIPS VLVETAFISN PEEEAKLRSR AYQDELADAL
MRGILRYFAA NPPLARSRPL
//
