ID   Y600_TREPA              Reviewed;         450 AA.
AC   O83609;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Putative zinc metalloprotease TP_0600;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=TP_0600;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65573.1; -; Genomic_DNA.
DR   PIR; B71304; B71304.
DR   RefSeq; WP_010882046.1; NC_021490.2.
DR   AlphaFoldDB; O83609; -.
DR   SMR; O83609; -.
DR   IntAct; O83609; 1.
DR   STRING; 243276.TPANIC_0600; -.
DR   EnsemblBacteria; AAC65573; AAC65573; TP_0600.
DR   KEGG; tpa:TP_0600; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_0_0_12; -.
DR   OMA; QYMVGFG; -.
DR   OrthoDB; 1395197at2; -.
DR   Proteomes; UP000000811; 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; -; 2.
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; 2.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   TIGRFAMs; TIGR00054; TIGR00054; 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..450
FT                   /note="Putative zinc metalloprotease TP_0600"
FT                   /id="PRO_0000088474"
FT   TRANSMEM        102..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          200..278
FT                   /note="PDZ"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   450 AA;  49565 MW;  7692F518985D37E7 CRC64;
     MIKIIIGVVV LGIVVLFHEL GHFVAALWCR VEVLSFSVGM GPVLFRKKFG KTEYRLSMLP
     LGGYCGMKGE QAFQTALDQK LSRIPVEPGS LYAVGPLKRM GIAFAGPLAN VLMAVMVLAL
     VSALGSRVHT FGNRISPVYV YDSSDNSPAR RVGLQDGDTI LRIGDQPIRY FSDIQKIVSQ
     HAQRALPFVI ERRGQLMHVT ITPDRDAHTG MGRVGIYHYV PLVVAAVDAH GAASRAGLEP
     EDKILAVAGR RVQHAVQLLA LLKEFRKKSV VLTVLRSGKR RYHTIALVRT ENGAIDVGIE
     WKAHTVVIPG TSFFASVRAG IAETLRMCVL TVKGIGMLFR GLQFQQAISG PLRITHVIGD
     VAQHGFQESF LTGLSQLCEF VALVCVSLFI MNLLPIPILD GGLILFACVE LFMQRSIHPR
     VLYYLQFVGF AFVALIFLCA FWNDVNFLFH