ID A0A0A7FZU1_9CLOT Unreviewed; 392 AA.
AC A0A0A7FZU1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:AIY84440.1};
GN ORFNames=U729_2137 {ECO:0000313|EMBL:AIY84440.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY84440.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY84440.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY84440.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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DR EMBL; CP006905; AIY84440.1; -; Genomic_DNA.
DR RefSeq; WP_039314695.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FZU1; -.
DR STRING; 1561.NPD11_880; -.
DR KEGG; cbv:U729_2137; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OrthoDB; 9776731at2; -.
DR Proteomes; UP000030635; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03886; M20_Acy1; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 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:AIY84440.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030635}.
FT DOMAIN 182..279
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 392 AA; 42635 MW; 659874CF804BD712 CRC64;
MNYWERAKEL KDEIISFRRN LHSNAEVGMN LPSTTEFVMK KLKSFGYEPT QIIDSGVVAT
IGNGQDPCIL LRADMDALPM TEESGLSFCS KNPRSAHTCG HDLHASMLLG AAKMLKENEE
NINGTIKLMF QPGEETFQGA KAMIDAGILE NPHVDRALSF HVGAGKAPVG VCAYNDKDAA
MFSSTGFKIN IKGKGSHGAT PHESIDSLNI AVHIYLALQE LIARETNPST PALLTIGQIS
GGSTSNIIPE TTMMQGTMRT VSKETDEYLK NRIVEVANGV AATFRGEATV SWLPSVPPLI
CDPEFTREML GYMKELDIPG FMPVGDTTAS ASEDFAIVLN HVPGTYMFLS AGFTDKESYT
AHNPKVLFNE DVLPEGSAFF AHCATRYLEN AN
//
