ID R9KAY2_9FIRM Unreviewed; 437 AA.
AC R9KAY2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=C809_03807 {ECO:0000313|EMBL:EOS43589.1};
OS Lachnospiraceae bacterium MD335.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235793 {ECO:0000313|EMBL:EOS43589.1, ECO:0000313|Proteomes:UP000014081};
RN [1] {ECO:0000313|EMBL:EOS43589.1, ECO:0000313|Proteomes:UP000014081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COE1 {ECO:0000313|EMBL:EOS43589.1,
RC ECO:0000313|Proteomes:UP000014081};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium COE1.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:EOS43589.1}.
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DR EMBL; ASSW01000059; EOS43589.1; -; Genomic_DNA.
DR AlphaFoldDB; R9KAY2; -.
DR STRING; 1235793.C809_03807; -.
DR PATRIC; fig|1235793.3.peg.3964; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG5632; Bacteria.
DR HOGENOM; CLU_042024_3_0_9; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000014081; Unassembled WGS sequence.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
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; 1.10.530.10; -; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR InterPro; IPR003646; SH3-like_bac-type.
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 Pfam; PF01832; Glucosaminidase; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51781; SH3B; 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:UP000014081}.
FT DOMAIN 372..437
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 437 AA; 47721 MW; E89F36AA90175772 CRC64;
MNLKQNYLTE SGCYKAGKHI TMKGLMIHSV GCPQPKADVF MKNWNRADAN ACVHAIVEPD
GDVYQLLPWD FRGWHCGGGA NNTHIGVEMT EPATIRYTGG SNWTETGNGE KTKAHVLAAY
KCAVELFAYL CQHFHLDPLA DGVIISHSEG CKRGIASNHG DVEHLWSKFG LLMGQFRKDI
GAAMEGGSAE DTLTAIMGKA KATAEQMKSY LQKKNPAVPQ SILDMVPLYL SEGEAEGVRG
DIAFAQSCLE TGNFTFSGSA VTLPQNNFCG LGVTQRGKTG LSFETAQLGI RAQIQHLKAY
ASTDALVNEK NDPRFRYVTR GCAPYAEWLG QKENPQGKGW AAGEKYGEKI LSILKAIVSE
GKVQFMESLT LSAPYMVRVS IPDLNIRRGP GTSYPKTGKF TGVGIFTVVE EKDGWGLLKA
YAEKRNGWIS LAFTTRM
//
