ID A0A095Y707_9BACT Unreviewed; 439 AA.
AC A0A095Y707;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KGF17811.1};
GN ORFNames=HMPREF1640_05605 {ECO:0000313|EMBL:KGF17811.1};
OS Prevotella sp. S7-1-8.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF17811.1, ECO:0000313|Proteomes:UP000029597};
RN [1] {ECO:0000313|EMBL:KGF17811.1, ECO:0000313|Proteomes:UP000029597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF17811.1,
RC ECO:0000313|Proteomes:UP000029597};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-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:KGF17811.1}.
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DR EMBL; JRNC01000032; KGF17811.1; -; Genomic_DNA.
DR RefSeq; WP_036893016.1; NZ_JRNC01000032.1.
DR AlphaFoldDB; A0A095Y707; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000029597; 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:KGF17811.1};
KW Protease {ECO:0000313|EMBL:KGF17811.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029597}.
FT DOMAIN 20..159
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 169..374
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 439 AA; 49542 MW; 66D52190503874A6 CRC64;
MKYNTATLSN GLRVIHMPSS SPVVYCGYCI RAGSRNERPG EEGLAHFCEH ATFKGTERRR
SWNVLNCLES VGGDLNAFTT KEDTTYHAAV LKQDISRAID ILTDIVFHST YPQGEIDKEV
EVICDEIESY NDTPSELIYD EFENLVFDGH PLGHAILGTT TNVRGFDTKK AHEFTNRFYK
PRNSVFFVYG DLSFKRIINK LCAVHQAKMV ETAGPKARAD DASPEKDKGL HTGCGGIQDI
GNDAHDGDKH VWLDKLAGQK TIVRKGTHQA HVMVGSRAYD IYDRRRMALY LLNNMIGGPG
MNTRLNLILR EHHGLVYTVE SSMVSYGDTG VWCTYFGCDP HDVDRCLRLV RRELDGFMQN
PISPTRLNAA KKQLKGQIGV ACDNRESFAL DFGKSFLHYG WEKDINQLYK NIDELTADNL
HEVANDIFNE SRLTTLIYK
//