ID   Q8G788_BIFLO            Unreviewed;       292 AA.
AC   Q8G788;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   OrderedLocusNames=BL0384 {ECO:0000313|EMBL:AAN24220.1};
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24220.1, ECO:0000313|Proteomes:UP000000439};
RN   [1] {ECO:0000313|EMBL:AAN24220.1, ECO:0000313|Proteomes:UP000000439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; AE014295; AAN24220.1; -; Genomic_DNA.
DR   RefSeq; NP_695584.1; NC_004307.2.
DR   RefSeq; WP_011068463.1; NC_004307.2.
DR   AlphaFoldDB; Q8G788; -.
DR   STRING; 206672.BL0384; -.
DR   EnsemblBacteria; AAN24220; AAN24220; BL0384.
DR   KEGG; blo:BL0384; -.
DR   PATRIC; fig|206672.9.peg.1124; -.
DR   HOGENOM; CLU_082946_0_0_11; -.
DR   OrthoDB; 9758772at2; -.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000439}.
FT   DOMAIN          12..147
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   292 AA;  31363 MW;  29B5775536E66A42 CRC64;
     MVGYAKAVWR GSPNHYQGRN GYKVTHITLH IMVGSLQGTD TVFQRSSYRA SSTYGVGTDG
     TVYQWVDEIN GAWCDANMAS DCSGISIEHA GGIAGIAPTD AEYEASAQLC ADIARRYGWT
     KLWHDETGNR TGNIVLHREV PGTDHAGCPD RAVNGLDVAR VINRANQILN NQGGTDMSCA
     LMIRDDDTGV VYYWSPETGR IGLGHPDQMK VLEDAGVKLI HSSKKATWAA RADQISGYVQ
     AKTTAYEKAQ TAALEALAKS VGANPSDITK TVSEAVNAAL KNLTVTLTNK EA
//