ID Q891H7_CLOTE Unreviewed; 446 AA.
AC Q891H7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Putative amino acid amidohydrolase {ECO:0000313|EMBL:AAO36868.1};
GN OrderedLocusNames=CTC_02398 {ECO:0000313|EMBL:AAO36868.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36868.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO36868.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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DR EMBL; AE015927; AAO36868.1; -; Genomic_DNA.
DR AlphaFoldDB; Q891H7; -.
DR STRING; 212717.CTC_02398; -.
DR MEROPS; M20.020; -.
DR KEGG; ctc:CTC_02398; -.
DR HOGENOM; CLU_023257_2_1_9; -.
DR OrthoDB; 9776731at2; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd05665; M20_Acy1_IAAspH; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR033845; AbgA.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR30575:SF3; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AAO36868.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT DOMAIN 245..333
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 446 AA; 49739 MW; 47A6F2837376D0BC CRC64;
MIMYTWGDRM FKWNYINNFI NDSYEEAVDI RRDIHKYAEY GWTEFRTASK IAEYLKNIGV
KVEIGEQNFN KEFMFGLPKK EELERHKNRA IEQGALEKYV NKMQGGFTGV VGIVETGIPG
PTTAFRFDID ANEGIESNSL DHRPVKEGFA SINDGAMHSC GHDGHISIGL ILAKTLMNIK
DNLKGTIKFI FQPAEEGVRG AYSMVNKGVV DNIDYFLTGH IGFTANKLGQ IITDTKGFLA
TTKLDVHFKG RSSHAGASPE KGKNALLAAA TAALNLQSFS QHGEGASRVN VGVLNAGTGR
NVIPEQAEMK IETRGENNNI NNYLENKARE VIKGAATMYD LDYEIIVAGS ADSAKSDEDF
SKIINKQLER IEEVKEIINS NRFSGSEDAT YMMNRVQENG GKAVYMIFGT EKSADHHNNS
FDFDERVLRI AIKVYAFITI YLNGME
//
