ID A0A081P9X4_9BACL Unreviewed; 416 AA.
AC A0A081P9X4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KEQ27497.1};
GN ORFNames=ET33_19840 {ECO:0000313|EMBL:KEQ27497.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ27497.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ27497.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ27497.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KEQ27497.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNVM01000003; KEQ27497.1; -; Genomic_DNA.
DR RefSeq; WP_036676331.1; NZ_JNVM01000003.1.
DR AlphaFoldDB; A0A081P9X4; -.
DR MEROPS; M16.A15; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000028123; 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: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:KEQ27497.1};
KW Protease {ECO:0000313|EMBL:KEQ27497.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028123}.
FT DOMAIN 12..158
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 165..337
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 416 AA; 46325 MW; AF84E1817BFFD133 CRC64;
MDKYTLTNGL RLVIEKIPTC RSVAFGIWVK TGSRSENETN NGISHFIEHM LFKGTEKYSA
KDIAEIFDGI GGNVNAFTSK EYTCYYCKVL DEHLPLAVEV LSDMFFGSVF DGTELEKEKN
VIYEEIAMYE DTPDDMVHDL IARAAFGGHS LGRTIIGTQS NLAAMTSDTL KEYMKSHYTI
ANTVISIAGN INDDVVGLIE KHFGSFANVG SQAPLEPLTF RSDSEYHQKK TEQNHICLSL
PGLAAKDDRL YAMILLNNAI GGGMSSRLFQ EIREKRGLAY SVYSYHSSYQ DGGLFTVYTG
TAPKQTEEVL KVTLELLADI KEKGLTPTEL KKGKEQMKGS LILSLESTSS RMNRIGKNEL
MLGRHYNLDE MIQRIESVEM EHVQALTAEL LSVPFALAMV GQTNEAIAGF RRDQLV
//