ID E0E2R2_9FIRM Unreviewed; 630 AA.
AC E0E2R2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EFM64827.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EFM64827.1};
GN ORFNames=HMPREF0634_0352 {ECO:0000313|EMBL:EFM64827.1};
OS Peptostreptococcus stomatis DSM 17678.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM64827.1, ECO:0000313|Proteomes:UP000003244};
RN [1] {ECO:0000313|EMBL:EFM64827.1, ECO:0000313|Proteomes:UP000003244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM64827.1,
RC ECO:0000313|Proteomes:UP000003244};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-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:EFM64827.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADGQ01000044; EFM64827.1; -; Genomic_DNA.
DR RefSeq; WP_007789216.1; NZ_ADGQ01000044.1.
DR AlphaFoldDB; E0E2R2; -.
DR STRING; 596315.HMPREF0634_0352; -.
DR GeneID; 84800526; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG2247; Bacteria.
DR OrthoDB; 9772024at2; -.
DR Proteomes; UP000003244; 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; 3.40.50.12090; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR007253; Cell_wall-bd_2.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30032:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE CWLM; 1.
DR PANTHER; PTHR30032; N-ACETYLMURAMOYL-L-ALANINE AMIDASE-RELATED; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF04122; CW_binding_2; 3.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EFM64827.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003244};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..630
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038519535"
FT DOMAIN 508..626
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 404..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 67031 MW; A12BCBEF69DBE95B CRC64;
MKVFLKRIMA MTLAVTILAA LTPYSLANEV NASDTGSKIE ASSSNNGSED QSGVMKIKLG
VAKLDQDGNV SEYLDAEEGD LSYEEKLDSN YAKSNANVSY LYGSDRYETS IQVSKASYPN
GADTVVLVNS SNAIYGLIAT PFASLNKAPI LLTSAKAIKP SVLDEIKRLK PKRVYMIGDT
SHISKGISNV IKANTGAEMA RIFGKNPSDL SAAVAEKISS SRKVNTAYLV STEYGVADAL
SISSRAGSTM APVLVASKNY VNSGVYNYLK NSADNVYYIG GQDSISNSLI NKISSVVRNG
GQANRIYGND RYQTNIKVIN KFYRNSDITS LIVTKAENNG LIDTVSAGPF ATLKSCPILI
THRNKLAVAS QNFLNKVQGN AIYQIGGGIS ASVTNLIKSG FQSAPTGSGT IETNPKPEDK
SKEKPNKKPG NNGGDNNVTP SKGIKGKTIV IDPGHGGKDS GAVGLNGYKE KDWTLKTALA
CADYLTKAGA DVVMTRKNDT YPTLQDRADI SNNSKAVLFC SIHYNKGGDV INPDTGEQSG
NGVEVYTGEG SFAQNTAKKV LNSILSKFNM KNRGVKDGTH LYVISNTLAP AILVEGGFMS
NSHDVNQLKS DEALRTMGIQ IAKGIIAAFN
//
