ID   Y890_THEMA              Reviewed;         501 AA.
AC   Q9WZZ2;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Putative zinc metalloprotease TM_0890;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=TM_0890;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD35971.1; -; Genomic_DNA.
DR   PIR; C72321; C72321.
DR   RefSeq; NP_228698.1; NC_000853.1.
DR   RefSeq; WP_004080697.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WZZ2; -.
DR   STRING; 243274.THEMA_00185; -.
DR   EnsemblBacteria; AAD35971; AAD35971; TM_0890.
DR   KEGG; tma:TM0890; -.
DR   eggNOG; COG0750; Bacteria.
DR   InParanoid; Q9WZZ2; -.
DR   OMA; YSRIVGW; -.
DR   OrthoDB; 1395197at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..501
FT                   /note="Putative zinc metalloprotease TM_0890"
FT                   /id="PRO_0000088473"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        474..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..180
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   501 AA;  55876 MW;  CE3E581117DC2A9A CRC64;
     MVIVYFILIL TGVIMVHELG HYLFARLFKV KVLEFAIGFG PKIFSVKGRE TTFRLNVFPI
     GGYVRMLGEE GEEIADEEEK EKSFYAKPAW QRFLITLAGP LFSILAGYLL FLPITLNWGI
     ALPGIDEVVP GSPAEEAGLR RGDIIYSIND KIAFDTSIIS NEIQKGLPVE LVIIRNGEKK
     SLRLTPRMYP ETYEFVLESA EGTPSGKLVS VNGNRDTSVL KEFVNEYVVL EFEGGTVKGI
     LKQFNEIPAR YMIGISFSGL APVFKKDIYF KEGLFVFKKG DRIVRVEDQE IEGWQDLVVL
     YQRLTLGKDT MIVSLQGENI EWWRGLSGSV RVVIKRGDST IEKNVEASFL KNILETPDLL
     EMGVPRYKPK NPLEAVNLSV KACNYVLLTT ASSLKNFFRN VQTGQIVGVV GLAGVISAAS
     KTGLEAVLTV VAVITISLGV LNLLPLPALD GGRIIFSLVE MITRKKLNPQ VENIIHFLGF
     IFLMILFLYI TFLDIGRMMG I