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Database: UniProt
Entry: A0A095Y707_9BACT
LinkDB: A0A095Y707_9BACT
Original site: A0A095Y707_9BACT 
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
//
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