ID A5I736_CLOBH Unreviewed; 975 AA.
AC A5I736; A7G8C0;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:CAL84869.1};
GN OrderedLocusNames=CBO3311 {ECO:0000313|EMBL:CAL84869.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL84869.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL84869.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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DR EMBL; AM412317; CAL84869.1; -; Genomic_DNA.
DR RefSeq; WP_012048254.1; NC_009698.1.
DR RefSeq; YP_001255795.1; NC_009495.1.
DR RefSeq; YP_001389035.1; NC_009698.1.
DR AlphaFoldDB; A5I736; -.
DR GeneID; 5186419; -.
DR KEGG; cbh:CLC_3253; -.
DR KEGG; cbo:CBO3311; -.
DR PATRIC; fig|413999.7.peg.3287; -.
DR HOGENOM; CLU_009165_1_0_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 464..714
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
FT COILED 475..517
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 975 AA; 113637 MW; 2EC628403635D638 CRC64;
MNLKLEEVYN GFKLINEEEI KEINSLAQVF LHEKSGAKLL FIKNDDDNKI FSISFRTPPK
DSTGVAHILE HSVLCGSRKF PVKEPFVELI KGSLNTFLNA MTFPDKTMYP VGSTNDKDFT
NLMDVYLDAV LYPNIYKYPE IMMQEGWHYE IENKNDDITY KGVVYNEMKG AFSSPESILF
RKIQESLLPD TVYGVESGGD PDYIPDLTQE DFKEFHKKYY HPSNSYIYLY GDLDILEKLK
FIDENYLKDF DKQEVDSKIK PQETFKDPKY MEIKYPISKE EKSEDKTYLS LNFSVGKSID
KELYLAFEIL EDILLETPSS PLKKALLDAG LGKDVFGVYD NSILQSTISI IVKNSNADKV
EEFKSVVFNT LQNLVKEGID KKLIESSINI KEFSLREADY QGYPKGLIYN IKSMESWLYD
EEPTVHLKYE DVLQKVKSAL NSNYFEDLIQ RYILDNNHYS VLLVKPEKGL EESRIENIRK
KLKDYKESLT EEELELLIKQ TKKLKERQNQ KDSMENLSKI PLLSIEDINK QAERLPLEEK
NILGIKTLYH NVFTNKISYL NLYFNTRAVE KEKIPYIGLL SAVLGKVSTE NYNYQDLSNE
VNISTGGIRY NAEIFSQKES HEDYKAMFTI KSKCLTSNVK ELMKLLSEIL TNSKFHEKNR
LREIIQELKS RLEMIMFDKG HTVAVKRLFS YFSSYGKYDE LLSGVEFYKF IVDIEKNFED
RFEDVSKNLQ NVFNKIFNST NLLVSVTGEK EEFSEVNKEF KILYDSLKEE KLQYNNYEFD
FDNSNEAFST SSKVQYVAKG YNYLKLGYKY SGSMQVLRTI VNYDYLWNKI RVQGGAYGAS
ASFIKNGNMF FASYRDPNLI KTIEAYDEAF KYVSQFNPED REMTKYIIGT ISDLDTPLTP
SAKGVRATEN YLRKISYEDR QREREDILST NKETIKAFSD VIKDLMKENY ICVIGNEDKI
KENKDKFNNI INLFE
//