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Database: UniProt
Entry: Q8XP50_CLOPE
LinkDB: Q8XP50_CLOPE
Original site: Q8XP50_CLOPE 
ID   Q8XP50_CLOPE            Unreviewed;       313 AA.
AC   Q8XP50;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Probable N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:BAB79821.1};
GN   OrderedLocusNames=CPE0115 {ECO:0000313|EMBL:BAB79821.1};
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB79821.1, ECO:0000313|Proteomes:UP000000818};
RN   [1] {ECO:0000313|EMBL:BAB79821.1, ECO:0000313|Proteomes:UP000000818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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DR   EMBL; BA000016; BAB79821.1; -; Genomic_DNA.
DR   RefSeq; WP_011009622.1; NC_003366.1.
DR   AlphaFoldDB; Q8XP50; -.
DR   STRING; 195102.gene:10489359; -.
DR   KEGG; cpe:CPE0115; -.
DR   HOGENOM; CLU_014322_3_1_9; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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:SF5; AUTOLYSIN PH-RELATED; 1.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..313
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039602573"
FT   DOMAIN          189..308
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          27..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  34503 MW;  D8E3AD96230A8A97 CRC64;
     MKKFLRILSI IIISSLMLLG CGSNSTKPDI NKDSNSINNS NEENNDTEKN NSNNENNNTE
     KNDSKEGNID QEKEKNKIDS NTDKETDKKN DVEPYCENEP NKANKDITIV IDPGHSSTIS
     NETEPECPGS QKRKLKDTLG ATGVQSKIPE YTITHGVAEE LKKLLISEGY NVIMTKDSPD
     KQLSNIERTT IGNDNNANLI IRIHCDGVDS PKACGASILV PATKGNVTKD ISDISYSYGE
     KILTAYTKYT GLKNRGVVVR DDLTGFNWSK VPIVLIELGF ISNPNEDSYL SNPDNYIKIA
     TGISNGINYC FAK
//
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