ID A0A0C1U2A0_9CLOT Unreviewed; 405 AA.
AC A0A0C1U2A0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:KIE46969.1};
GN ORFNames=U732_1433 {ECO:0000313|EMBL:KIE46969.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE46969.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE46969.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE46969.1,
RC ECO:0000313|Proteomes:UP000031366};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE46969.1}.
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DR EMBL; AYSO01000015; KIE46969.1; -; Genomic_DNA.
DR RefSeq; WP_039632421.1; NZ_AYSO01000015.1.
DR AlphaFoldDB; A0A0C1U2A0; -.
DR STRING; 29341.RSJ17_13055; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
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:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000031366}.
FT DOMAIN 17..149
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 163..341
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 405 AA; 47195 MW; 1F0D76B668814448 CRC64;
MKKIFLKNKL KFIYTHSENT ITSFTIGLNA GAIVEDGNEV GLAHVVEHMV FKGTKNRSEA
EINNQCDKIF GFHNAMTNYP YVVYYGTCLS EDFEKGLEIY SDILLNPTFK EEHFKEEISV
ICEELKEWSD DTSQFCEDKV LFNGFTHRRI KDLIIGNEDV IKSFTINDVK GFYDKYYIPN
NCTISVVSSL CFEDVYKIID RYFSQWEEEK YENNEIVYEE NTCGTFVEEK NDINSCKIQY
IFPIHNLNQR EITLLRIFNS FFCEGTSSIL YDEIRTKRGL VYDISSKLKN ENGIKLYTII
LGTSKENVNT SIEIINNEIE KVKVLDGYFT EEKIKNIIKS LKLKRILGLE KSISLSFNIC
IFDIMYGDYN ILFNEYDIED ITENEILKVA NKVLKNPTIQ IIKSK
//
