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Database: UniProt
Entry: R5P337_9FIRM
LinkDB: R5P337_9FIRM
Original site: R5P337_9FIRM 
ID   R5P337_9FIRM            Unreviewed;       258 AA.
AC   R5P337;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CCZ03502.1};
GN   ORFNames=BN730_00338 {ECO:0000313|EMBL:CCZ03502.1};
OS   Eubacterium sp. CAG:603.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262891 {ECO:0000313|EMBL:CCZ03502.1, ECO:0000313|Proteomes:UP000018312};
RN   [1] {ECO:0000313|EMBL:CCZ03502.1, ECO:0000313|Proteomes:UP000018312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:603 {ECO:0000313|Proteomes:UP000018312};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCZ03502.1}.
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DR   EMBL; CAZI010000022; CCZ03502.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5P337; -.
DR   Proteomes; UP000018312; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018312};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          131..247
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   258 AA;  28445 MW;  D967321C677A121A CRC64;
     MQSSRKAKNI QLIRFVIGIL LCSAIILFVY MLLPDSRSET GNAGHSMLLS SSTISEAEEL
     SSTVRLPLSD CEVCIDAGHG GQDIGSSKGK RLEKDDTLDL SMKIFKYLSD KGISVAISRT
     NDTYLSLQER KDFAEDSNCT LFISIHRNLY EGNSKINGAE AWIHSSDPVN AHSLASSILN
     DICSSNNFDN PTFDNRGVKC GTSSDAYDNY AINKVSMTSM ILEMGFITSP YDNRAFDNNL
     DTYAKIIGDD IIDYLNNK
//
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