ID   D7JF39_9BACT            Unreviewed;       975 AA.
AC   D7JF39;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:EFI16850.1};
GN   ORFNames=HMPREF0156_00438 {ECO:0000313|EMBL:EFI16850.1};
OS   Bacteroidetes oral taxon 274 str. F0058.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=575590 {ECO:0000313|EMBL:EFI16850.1, ECO:0000313|Proteomes:UP000004685};
RN   [1] {ECO:0000313|Proteomes:UP000004685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0058 {ECO:0000313|Proteomes:UP000004685};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroidetes bacterium Oral taxon 274 strain
RT   F0058.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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; GG774889; EFI16850.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7JF39; -.
DR   STRING; 575590.HMPREF0156_00438; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_306466_0_0_10; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000004685; Unassembled WGS sequence.
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; 4.
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; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
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:EFI16850.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004685};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..975
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003100279"
FT   DOMAIN          58..113
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          150..247
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          262..432
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          725..866
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   975 AA;  111230 MW;  8FE3DDECB1C12B3C CRC64;
     MLKRNLFLSL FAIALSLSVY GQTYQWKEAR SGGYTYKYVT HDPTNARFYT LRNGLTVILS
     PTNKEPRIQC YMAVKAGSKT DPATNTGLAH YLEHLLFKGT DKYGSLDWEK ESKELDKIDD
     LYEQYNKTKD ADRRKAIYKK IDSVSGVASK YAIANEYDKM MTSMGAQGTN AFTSFEKTVY
     TDDVPANALD KYITVQAERF RNPVLRIFHT ELEAVYEEKN RSLDSDGSQV FETLFANLFK
     KHNYGLQTTI GTVEHLKNPS LREIRKYFKT YYVPNNMAVV LSGDFNPDEV IAKIDKAFSY
     MEYKDVPKYT FEKEDPITAP IVREVVGPDA ESVSIAYRLP GNQEKDALLA DLVGEILTNG
     EAGLIDLNLV KKQKLLGASA FNWALIDYGV LWLSGRPSQG QSLEQVKDLM LNEIENLKKG
     NFDDDLIPSI VNNIKKRIIQ STESYSSRAY MLMNAFTDNL DWRDQVAYVN DLSKIKKQDV
     VAFANKYLGN NYVVVYKKQG QRTNVEKIEK PAITPVETNA DKQSAFVKMV NDMPSTPVSP
     VFLDYNKDLQ KSKLGKAEVL YVQNKDNDLY RLRFRYKIGY LNDLKMPLVS DYIEFLGTDK
     KSAEQISKEF YKIASSFRIS VGEEYTTVTI EGLQENFEAA VKLYEDLVLN VKADNEALAA
     LKARLTKSRT DAKANRATIM QALTSYALYG AKNKFNNRLS DAEIESVTAK ELVDRVKNLN
     NVEQTVIYYG PSTLAELTAK LKPLHKVPAT FAKVAPKKEF KQVEQTKNQV LFTDYEMVQA
     ETRWIRNTNT YNPAENTVIS VFNNYFGGGM GSLVFQTIRE SKALAYSTYG FYVFPRKKAD
     KYYMMAYVGA QADKFVEAVA AMNELLTTMP ELPANLDLAK VQLKKEIQTE RITQDDIIYD
     YIKAKDLGLN EDIRKTIYQN LDNISMKDIR TFHDTYLSKK PYTYVVLASE EKLSKEELQK
     IGEFRKLSLE ELFGY
//