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Database: UniProt
Entry: E5B259_ERWAM
LinkDB: E5B259_ERWAM
Original site: E5B259_ERWAM 
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};
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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
//
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