ID C0EVV9_9FIRM Unreviewed; 265 AA.
AC C0EVV9;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EEG36602.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EEG36602.1};
GN ORFNames=EUBHAL_01547 {ECO:0000313|EMBL:EEG36602.1};
OS Anaerobutyricum hallii DSM 3353.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerobutyricum.
OX NCBI_TaxID=411469 {ECO:0000313|EMBL:EEG36602.1, ECO:0000313|Proteomes:UP000003174};
RN [1] {ECO:0000313|EMBL:EEG36602.1, ECO:0000313|Proteomes:UP000003174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG36602.1,
RC ECO:0000313|Proteomes:UP000003174};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG36602.1, ECO:0000313|Proteomes:UP000003174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG36602.1,
RC ECO:0000313|Proteomes:UP000003174};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium hallii (DSM 3353).";
RL Submitted (FEB-2009) 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:EEG36602.1}.
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DR EMBL; ACEP01000070; EEG36602.1; -; Genomic_DNA.
DR AlphaFoldDB; C0EVV9; -.
DR eggNOG; COG0860; Bacteria.
DR Proteomes; UP000003174; 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:EEG36602.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..265
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039135319"
FT DOMAIN 143..261
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 35..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..60
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 29007 MW; 6C15304A411609A7 CRC64;
MMKKTFSLLM IFMLVFTMIP TSTLKVSAKA AAATTQAKKA TTKTAKKTAK KKKKTKAKKQ
RTVFIAAGHQ QRGISSTERL APGSSRRKAK LTSGTAGVRT HIPEYKTNLA IAKATKKELK
KRGYKVIMLR TTNNCPLSNQ QRTKKANKSG ADIHICIHCN ASGASARGPL VCVPGSSRYV
GKKIFNSSRR LGSCLLSSVA KAVNKKSHGT IRSDYYTTIN WAKIPTMILE CGFLTNPTED
RQLNSSSYQK KLAKGIANGV DKYFK
//
