ID A0A1E8EYM9_9CLOT Unreviewed; 540 AA.
AC A0A1E8EYM9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase LytC {ECO:0000313|EMBL:OFI06056.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:OFI06056.1};
GN Name=lytC_5 {ECO:0000313|EMBL:OFI06056.1};
GN ORFNames=CLOACE_13110 {ECO:0000313|EMBL:OFI06056.1};
OS Clostridium acetireducens DSM 10703.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI06056.1, ECO:0000313|Proteomes:UP000175744};
RN [1] {ECO:0000313|EMBL:OFI06056.1, ECO:0000313|Proteomes:UP000175744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI06056.1,
RC ECO:0000313|Proteomes:UP000175744};
RA Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium acetireducens DSM 10703.";
RL Submitted (JUN-2016) 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:OFI06056.1}.
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DR EMBL; LZFO01000016; OFI06056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E8EYM9; -.
DR STRING; 1121290.CLAOCE_13110; -.
DR PATRIC; fig|1121290.3.peg.1290; -.
DR Proteomes; UP000175744; 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; -; 3.
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:OFI06056.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000175744};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009213716"
FT DOMAIN 433..538
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 332..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 59610 MW; 9A411B6AB2B76080 CRC64;
MLNKFCMFKK NLAFVVFILT MAISMKFNNV SAKYNFQKIK GQNRYETSFG IANEFQKGKV
DNVILSSGKD FPDALSGSVL SKKLNAPILL VENNLSKNSS AIKYIKNHLD KSGKIYILGG
NGSVSYSYES YFKKLGYNNV ERLWGKDRYE TNKNVVRKLN VPKGTPVVIV NGQAFPDALS
VSSAASINGY PILLNSKGDL SNQCKEILKS VNPDRVYLIG GQGVLSSNIE NEIKILISKT
PIRIYGKDRY ETCLSVNKYF NTNSSNVILA SGENFPDALS GTSLASKLKA PIILTNGYNL
SNQKQYIDSI KCSNIILLGA VNENIVDKLS KVEIKPEPKP EPKPSPKPEP KPEPKPEELN
SKPKESRLFN VNPGHTLTGR DTGAQGINGL REEVLTRELS EELIKELKAA GQSTNLVRVD
HADSLVESLN KQVAICESVN ADMNVVIHFN VSGGQGNGIE IFTYRGQYVK EADRVLKEME
KLGFTNRGIK NRSLALINNT KATTIYIEVC FIDNPHDVEL LNKYGMNGIA KAIVRGLLGK
//
