ID D7GRF8_9FIRM Unreviewed; 443 AA.
AC D7GRF8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CBL40383.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:CBL40383.1};
GN ORFNames=CK3_05810 {ECO:0000313|EMBL:CBL40383.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL40383.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL40383.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40383.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL40383.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40383.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FP929062; CBL40383.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GRF8; -.
DR KEGG; bprs:CK3_05810; -.
DR PATRIC; fig|245014.3.peg.2306; -.
DR HOGENOM; CLU_042903_0_0_9; -.
DR BioCyc; BBAC245014:G1314-481-MONOMER; -.
DR Proteomes; UP000008961; Chromosome.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
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 Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
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 Pfam; PF01832; Glucosaminidase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CBL40383.1}.
FT DOMAIN 6..185
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|Pfam:PF01520"
FT DOMAIN 241..322
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|Pfam:PF01832"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 48408 MW; C439E9689C84D91F CRC64;
MSKVKICIDA GHVGSNYNQS PVVKTYFESE AMWKLHLLLK AELKKKGFEV ITTRAKQEKD
LGVYQRGTAA KGCDVFLSLH SNACGTESVD YPVVYRAYDN LNKVNDLALA IAKKIGQLIG
TEQTGKTAIR KNDSGGEYYG VMRGARAVGV PLYMLIEHSF HTNKKATLWL SKEENLKRLA
VAEAELLAAH FKMEAKPESK EEGKVEIMGT AEATAAQMAL YCRSKNAAPK LTSCTLEELA
QMFLEEGKAE GIRGDIAFAQ SLKETGFFKY GGIVLPSQNN YAGIGALNGN GKGEAATFPT
PRIGVRAQIQ HLKAYASKKA LVNPCVDPRF HLVTRGSAPY VEWLGAADNP DGKGWAVPGK
GYGKSLLELL DAIKGTKPPQ KPQELPEEKP EDNIPKWQKE GFNALVEAGI INTPEYWEKK
LTQPITVGEA LGIIGRVYGM LDK
//
