ID E2SKM5_9FIRM Unreviewed; 231 AA.
AC E2SKM5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EFP61774.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EFP61774.1};
GN ORFNames=HMPREF0983_01622 {ECO:0000313|EMBL:EFP61774.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP61774.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP61774.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP61774.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) 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:EFP61774.1}.
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DR EMBL; ACTJ01000036; EFP61774.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SKM5; -.
DR STRING; 658659.HMPREF0983_01622; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_7_0_9; -.
DR BioCyc; EBAC658659-HMP:GMFE-1649-MONOMER; -.
DR Proteomes; UP000006223; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:EFP61774.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..231
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003164419"
FT DOMAIN 115..224
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 231 AA; 25823 MW; 4070C0B44D4243E7 CRC64;
MKIMKRKKYL LGAGLLCTIL AASLCLSHIT SVSAKRAFHA LDGVEIVLDP GHGGKDDGAR
SNEAKEQEIN LKIAQKLKKL LETGGAHVTM TREGAYDLAS ENATNRKRED MKKRMELINQ
EKTDLFLSIH LNSYPNTSVK GAQAFYAPKN EVSKVFADIL QKHLRALTQT KMTSKPGDYY
ILNNAEKIGS LVECGFLSNA EDRAKLITDE YQQKMAQTLY DSILEYFNFL S
//
