ID A0A0A7FW58_9CLOT Unreviewed; 435 AA.
AC A0A0A7FW58;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Processing protease {ECO:0000313|EMBL:AIY83822.1};
GN ORFNames=U729_2780 {ECO:0000313|EMBL:AIY83822.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY83822.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY83822.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY83822.1};
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).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP006905; AIY83822.1; -; Genomic_DNA.
DR RefSeq; WP_039316011.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FW58; -.
DR STRING; 1561.NPD11_247; -.
DR MEROPS; M16.A15; -.
DR KEGG; cbv:U729_2780; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_0_9; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000030635; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AIY83822.1};
KW Protease {ECO:0000313|EMBL:AIY83822.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030635}.
FT DOMAIN 13..159
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 165..338
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 435 AA; 49492 MW; 744E4E7BDCF5189A CRC64;
MHKIFTLKNG LRVVMDRIDG VNSVSVGVMI QNGSRNESLN LNGISHFIEH MFFKGTYNRS
AKEIAEEIEN VGGQINAFTS KEATCYYIKA LSTHLDISLD ILSDMLLNSK FDEGDIEKEK
GVVIEEINMN EDNPEDVLDN IHSKASFEEN SLSYPILGTI EKIRSLTRKD ILDFIEEKYT
PYNSVISICG KFDEEEVIKL VEKYFGKWES KKVYTPEYEG TEIKSNSVFI KKEIEQLHIG
LGIQGLPFED ERGYALVLLN NILGGGASSI LFQKVREELG LCYSIYSYPQ PFKKAGIVNI
YVGLSKEYAD KALKVIKREI ENFVQNGITD EELKINKEKI KASYILGLES TSSKMFANAK
SLLFRNRIRT EEDVIKKVDN ISKEDIEYVL KNCFGKGIIN TAYVGPEIDV DYLDSCIYKD
TEAYDNSRKT NKFKL
//
