ID A0A1V4J068_9CLOT Unreviewed; 353 AA.
AC A0A1V4J068;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase AmiA {ECO:0000313|EMBL:OPJ65415.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:OPJ65415.1};
GN Name=amiA {ECO:0000313|EMBL:OPJ65415.1};
GN ORFNames=CLCHR_08050 {ECO:0000313|EMBL:OPJ65415.1};
OS Clostridium chromiireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=225345 {ECO:0000313|EMBL:OPJ65415.1, ECO:0000313|Proteomes:UP000191056};
RN [1] {ECO:0000313|EMBL:OPJ65415.1, ECO:0000313|Proteomes:UP000191056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23318 {ECO:0000313|EMBL:OPJ65415.1,
RC ECO:0000313|Proteomes:UP000191056};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium chromiireducens DSM 23318.";
RL Submitted (MAR-2017) 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:OPJ65415.1}.
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DR EMBL; MZGT01000008; OPJ65415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4J068; -.
DR STRING; 225345.CLCHR_08050; -.
DR OrthoDB; 43070at2; -.
DR Proteomes; UP000191056; 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; 2.10.270.10; Cholin Binding; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
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; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51170; CW; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:OPJ65415.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191056};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 115..233
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REPEAT 265..284
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
SQ SEQUENCE 353 AA; 39178 MW; 0766B12E7B76B3C4 CRC64;
MKRLLTFFMT LIVLNIFTIG ISNNQIALAS GKKVVVIDPG HGTGGNREYE LQSPDSSITK
IKDGGGTQGV VTGVPEYVVT LKVAEKLKTL LEQKNYTVIM TKTQESEAPG NIERAEVGNN
NNADLVIRIH CDGMDNQSMT GASMLVPAPI GYAKDISSIS AQYGQTILND LISSAGMNNR
GVVQRSDLTG FNWSKVPVVL VEMGFMSNPG EDRLLSDDSY QNKLVQGLCN GIVHSLNKYE
LGWNQNSEGW WYCTDPDKGY YYTANNGWKY IDGQWYIFNS AGYALQSTWY TDPSNSHKYY
LDSNCMRVNG EKDKPKWVNI NDSYYGFNEE GQLYVNCKTP DGYNVNENGV ASN
//
