ID   Y210_RICTY              Reviewed;         412 AA.
AC   Q68XF0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Uncharacterized zinc protease RT0210;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=RT0210;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Binds Zn(2+). {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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; AE017197; AAU03692.1; -; Genomic_DNA.
DR   RefSeq; WP_011190678.1; NC_006142.1.
DR   AlphaFoldDB; Q68XF0; -.
DR   SMR; Q68XF0; -.
DR   STRING; 257363.RT0210; -.
DR   MEROPS; M16.016; -.
DR   EnsemblBacteria; AAU03692; AAU03692; RT0210.
DR   KEGG; rty:RT0210; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_0_5; -.
DR   OMA; IDVVCDM; -.
DR   OrthoDB; 1188251at2; -.
DR   Proteomes; UP000000604; Chromosome.
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   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   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..412
FT                   /note="Uncharacterized zinc protease RT0210"
FT                   /id="PRO_0000295171"
FT   ACT_SITE        52
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   412 AA;  46619 MW;  54CE545CE7096684 CRC64;
     MKENFNISKL KNGLTILTYN MPYVHSVAIN LIAKVGARYE NEEEEGISHF LEHMAFKGTK
     TRTAQQIAEE FDSIGGYFNA YTGYENTVYY VRVLSENCHK ALNILADIIQ NSIFADEEIS
     KEYQIIMQEI AHHHDNPDDL IYETFYNTVY KDQPLGKSIL GTAKTLVKFT QEHFLNFIGK
     HYNAENLYLS IAGNIEHNKI VIIAEELFAS LKQGVTSSFI PAKYIGGKGF IHKELEQTSL
     VLGFECTSYI NLEKLYQTYL LSIIFGGGVS SRLFQSIREK LGLAYVVGSY NSAYFDSGVF
     TIYASTAHEK LELLYSEIKN EIIKITETVS TEELMRAKIQ LRSNLQMAQE QNSYKSEEIG
     KNYSVFGKYI LPEEIIEIIT NIKADDIINT ANKIFSGTTA LAIIGPNDLN GF