Y3003_CLOBH
ID Y3003_CLOBH Reviewed; 228 AA.
AC A5I683; A7G7G6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=UPF0758 protein CBO3003/CLC_2900;
GN OrderedLocusNames=CBO3003, CLC_2900;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; CP000727; ABS38997.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL84565.1; -; Genomic_DNA.
DR RefSeq; WP_003360029.1; NC_009698.1.
DR RefSeq; YP_001255495.1; NC_009495.1.
DR RefSeq; YP_001388731.1; NC_009698.1.
DR AlphaFoldDB; A5I683; -.
DR SMR; A5I683; -.
DR GeneID; 5185046; -.
DR KEGG; cbh:CLC_2900; -.
DR KEGG; cbo:CBO3003; -.
DR PATRIC; fig|413999.7.peg.2981; -.
DR HOGENOM; CLU_073529_0_2_9; -.
DR OMA; AMPDYEL; -.
DR PRO; PR:A5I683; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08071; MPN_DUF2466; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR025657; RadC_JAB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001405; UPF0758.
DR InterPro; IPR020891; UPF0758_CS.
DR PANTHER; PTHR30471; PTHR30471; 1.
DR Pfam; PF04002; RadC; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR TIGRFAMs; TIGR00608; radc; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS01302; UPF0758; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..228
FT /note="UPF0758 protein CBO3003/CLC_2900"
FT /id="PRO_1000001651"
FT DOMAIN 106..228
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 177..190
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 228 AA; 25671 MW; 33AFFFCACBD752E5 CRC64;
MDNNFKIKDL PKNERPQERL IRYGAEVLSN SELLAVILRT GTKNQNIMML ASSLIKETGG
LDQLFNQSIE ELTKIKGIGV TKAVQILALS ELSKRFKTYK SGNEYKISTP LDVSNLVMED
MKYLKQEKLK ILILNTKNIV TYIRDVFIGT LNSSIVHPRE IFCEAIKKNG ASIIICHNHP
SGDPTPSKED INITLRLKEC GKLIGIDLLD HIIIGENKYV SMKEKGTI