ID   AMIB_BUCBP              Reviewed;         217 AA.
AC   Q89A33;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Putative N-acetylmuramoyl-L-alanine amidase;
DE            EC=3.5.1.28;
GN   Name=amiB; OrderedLocusNames=bbp_521;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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}.
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DR   EMBL; AE016826; AAO27223.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q89A33; -.
DR   SMR; Q89A33; -.
DR   STRING; 224915.bbp_521; -.
DR   KEGG; bab:bbp_521; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_4_1_6; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000000601; 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   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Reference proteome; Secreted.
FT   CHAIN           1..217
FT                   /note="Putative N-acetylmuramoyl-L-alanine amidase"
FT                   /id="PRO_0000164423"
FT   DOMAIN          3..206
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   217 AA;  25202 MW;  F967E3E50F4752A1 CRC64;
     MIIAIDAGHG GQDPGAIGKN KFQEKNITLS IAKKLTKLLN HTNFFKAVMI RRGNYFLSVF
     KRTQIAEKYH ANLLISIHAN SSKNRKISGV SIWVLPKNVH NTRIQKHKLN KKTKNIHKKI
     NTKTSKFKNF YEIEYDLAKI IIQELRKVST LNQKKPKYAK FGILKFSQFP SILVETGFIS
     NPIEEQHLNK KFYQNLISKS ISIALKKYFL KRIKQYN
//