AMIB_BUCAP
ID AMIB_BUCAP Reviewed; 233 AA.
AC Q8K908;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Putative N-acetylmuramoyl-L-alanine amidase;
DE EC=3.5.1.28;
GN Name=amiB; OrderedLocusNames=BUsg_555;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell
CC division. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
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; AE013218; AAM68093.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8K908; -.
DR SMR; Q8K908; -.
DR STRING; 198804.BUsg_555; -.
DR EnsemblBacteria; AAM68093; AAM68093; BUsg_555.
DR KEGG; bas:BUsg_555; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_4_1_6; -.
DR OMA; QIRPVHH; -.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR Pfam; PF01520; Amidase_3; 1.
DR SMART; SM00646; Ami_3; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Hydrolase; Secreted.
FT CHAIN 1..233
FT /note="Putative N-acetylmuramoyl-L-alanine amidase"
FT /id="PRO_0000164422"
FT DOMAIN 1..219
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000255"
SQ SEQUENCE 233 AA; 27259 MW; 4F492C6C2D5FF31E CRC64;
MIDPGHGGQD PGAINSLGLQ EKKITLKIGI KLKNLLQNSD LFYPVLTRND DSYVSLKKRR
DFLKNNHVSF LISIHADSSK KRYVSGASIW ITTNDRMHRE INNFIKNREE NIYFPKNIQN
LIQKNKHDFF LKKTVLDLQF NNFQKMEINL SRYIFQQLKK IIKLDKINLN YASLGILSSI
NTPSMLIETG FITNFLEEKK LRTNKYQNKI ANAIYIALKN YFQDRLLSNL RNT