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Database: UniProt
Entry: A0A0R2I215_9LACO
LinkDB: A0A0R2I215_9LACO
Original site: A0A0R2I215_9LACO 
ID   A0A0R2I215_9LACO        Unreviewed;       221 AA.
AC   A0A0R2I215;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KRN58814.1};
GN   ORFNames=IV45_GL000441 {ECO:0000313|EMBL:KRN58814.1};
OS   Limosilactobacillus secaliphilus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=396268 {ECO:0000313|EMBL:KRN58814.1, ECO:0000313|Proteomes:UP000050934};
RN   [1] {ECO:0000313|EMBL:KRN58814.1, ECO:0000313|Proteomes:UP000050934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17896 {ECO:0000313|EMBL:KRN58814.1,
RC   ECO:0000313|Proteomes:UP000050934};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRN58814.1}.
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DR   EMBL; JQBW01000009; KRN58814.1; -; Genomic_DNA.
DR   RefSeq; WP_057741035.1; NZ_JQBW01000009.1.
DR   AlphaFoldDB; A0A0R2I215; -.
DR   STRING; 396268.IV45_GL000441; -.
DR   PATRIC; fig|396268.3.peg.448; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000050934; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050934}.
FT   DOMAIN          106..215
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   221 AA;  24708 MW;  3BE9125D901D8C7A CRC64;
     MQEKNGWYKL RLTDHQVAWT PAWLIHSKRK LAKNDHIAGA TIVIDPGHGG ADSGAMANGS
     GRDKQNQEKT YTLRIANQLQ KSLIQQGARV IMTRDSDRYV SLESRVNLSN QRRADAFISL
     HLNSSPNENE GSGITTYYYH RGPSKQLAKS VSKQVNALPG KNLGIEFGDF EVLRDNHQPA
     ILCETGYINS SKDFKMIQKP SFQKKTAHAI TQGLNSFLQN N
//
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