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Database: UniProt
Entry: Q73H15_WOLPM
LinkDB: Q73H15_WOLPM
Original site: Q73H15_WOLPM 
ID   Q73H15_WOLPM            Unreviewed;       446 AA.
AC   Q73H15;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Protease, insulinase family {ECO:0000313|EMBL:AAS14451.1};
GN   OrderedLocusNames=WD_0761 {ECO:0000313|EMBL:AAS14451.1};
OS   Wolbachia pipientis wMel.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=163164 {ECO:0000313|EMBL:AAS14451.1, ECO:0000313|Proteomes:UP000008215};
RN   [1] {ECO:0000313|EMBL:AAS14451.1, ECO:0000313|Proteomes:UP000008215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMel {ECO:0000313|EMBL:AAS14451.1};
RX   PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA   Wu M., Sun L.V., Vamathevan J., Riegler M., Deboy R., Brownlie J.C.,
RA   McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA   Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA   Nelson W.C., Mohamoud Y., Lee P., Berry K., Young M.B., Utterback T.,
RA   Weidman J., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA   O'Neill S.L., Eisen J.A.;
RT   "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT   streamlined genome overrun by mobile genetic elements.";
RL   PLoS Biol. 2:327-341(2004).
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}.
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DR   EMBL; AE017196; AAS14451.1; -; Genomic_DNA.
DR   RefSeq; WP_010082492.1; NZ_OX384529.1.
DR   AlphaFoldDB; Q73H15; -.
DR   EnsemblBacteria; AAS14451; AAS14451; WD_0761.
DR   GeneID; 70036242; -.
DR   KEGG; wol:WD_0761; -.
DR   eggNOG; COG0612; Bacteria.
DR   Proteomes; UP000008215; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AAS14451.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          44..184
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          194..370
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   446 AA;  50570 MW;  8D728559A20A65C8 CRC64;
     MLHKFFSFLI LPVLFFTYPI SSNALNIEHN IKYTKLSNGL DVYVVSNHRI PAVLHAVIYK
     VGGMDDPIGK AGLAHYFEHL MFETTGKFTD IEATMSSIGA QFNAFTTKEY TCYFELIPKK
     DLPLAMEVEA DRMGSFNVTQ DKIDREKNIV LEERKMRFDN QPHNLLWEEM DSAFYRTGYG
     RSVIGWESDI KTYNLDDITR FHDNYYHSGN AILLIVGDVE LDEVVKLAEE KYGEIKAKPV
     MRNYPNQDPV HNAGLSVTLE STEVKESVLY FRYRVPLFDH INEASAAHLA VDILGGGKSS
     KLYKDLVLDK DVAVSVFAYY NSLAFSDGYI DIMIIPKSGA NLDIVERELD NAINGFVSKG
     VTSEELQSSK YRYKAAQFDN LSDLTHIAMF YVPHLALGIP LDEIDISYSK INDVNLEDVN
     NKIRAIFSAN KLIGRLLPKG DNNENK
//
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