ID E5B259_ERWAM Unreviewed; 415 AA.
AC E5B259;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, 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};
GN Name=amiC {ECO:0000313|EMBL:CBX79561.1};
GN ORFNames=EAIL5_0741 {ECO:0000313|EMBL:CBX79561.1};
OS Erwinia amylovora ATCC BAA-2158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX79561.1};
RN [1] {ECO:0000313|EMBL:CBX79561.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX79561.1};
RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT Restricted to Rubus Plants.";
RL J. Bacteriol. 193:785-786(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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR719187; CBX79561.1; -; Genomic_DNA.
DR AlphaFoldDB; E5B259; -.
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 InterPro; IPR006311; TAT_signal.
DR NCBIfam; NF038267; amidase_AmiC; 1.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CBX79561.1}.
FT DOMAIN 248..402
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 415 AA; 46007 MW; 8ACC3160C9BBD769 CRC64;
MTDSTSLNRR RLLQGAGALW LLSVSRTGMT ASRHVVAIRI WPASTYSRLT IESNAPLKYK
QFSLRSPDRV VVDIADIQLN RLLNDVGKLV REDDPYIKNV RVGQFDPNTV RLVLEIKQNV
APRIFTLAPV AGIKNRLVLD LYPVQRPQHN DDPLLALLED YNQGDLGRSQ PEAAPLPGKA
GKDRPIVIML DPGHGGEDSG AVGKQKTREK DVVLKIARRL KSLIDKQPNM RAYMTRNEDV
FIPLKVRVAK ARKQRADLFI SIHADAFTRR AARGSSVFAL STKGATSTAA RFLAQTQNES
DLIGGVSMGS DRYLDHTMFD MLQSRTINDS LRFGGEVLAR MGKINHLHKR SVDQAGFAVL
KAPDIPSILV ETAFISNLEE ERKLRTTRFQ HQVADSILAG IKAYFANGAA LATAK
//