(data stored in SCRATCH3701 zone)

SWISSPROT: Y210_RICTY

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   11-DEC-2019, entry version 74.
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}.
DR   EMBL; AE017197; AAU03692.1; -; Genomic_DNA.
DR   RefSeq; WP_011190678.1; NC_006142.1.
DR   SMR; Q68XF0; -.
DR   STRING; 257363.RT0210; -.
DR   MEROPS; M16.016; -.
DR   EnsemblBacteria; AAU03692; AAU03692; RT0210.
DR   KEGG; rty:RT0210; -.
DR   eggNOG; ENOG4108J6I; Bacteria.
DR   eggNOG; COG0612; LUCA.
DR   HOGENOM; HOG000242449; -.
DR   OMA; YTHILNH; -.
DR   OrthoDB; 1188251at2; -.
DR   BioCyc; RTYP257363:G1G0L-214-MONOMER; -.
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   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;
DR   PRODOM; Q68XF0.
DR   SWISS-2DPAGE; Q68XF0.
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   METAL           49
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   METAL           53
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   METAL           129
FT                   /note="Zinc"
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
//

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