ID   Y293_RICCN              Reviewed;         412 AA.
AC   Q92IX7;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Uncharacterized zinc protease RC0293;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=RC0293;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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}.
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DR   EMBL; AE006914; AAL02831.1; -; Genomic_DNA.
DR   PIR; E97736; E97736.
DR   RefSeq; WP_010976953.1; NC_003103.1.
DR   AlphaFoldDB; Q92IX7; -.
DR   SMR; Q92IX7; -.
DR   MEROPS; M16.016; -.
DR   EnsemblBacteria; AAL02831; AAL02831; RC0293.
DR   KEGG; rco:RC0293; -.
DR   PATRIC; fig|272944.4.peg.333; -.
DR   HOGENOM; CLU_009902_3_0_5; -.
DR   OMA; IDVVCDM; -.
DR   Proteomes; UP000000816; 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 RC0293"
FT                   /id="PRO_0000074426"
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;  46391 MW;  F46E72AB0E499DA5 CRC64;
     MKENFNVSKL KNGLTILTYN MPYVNSVAIN LIAKVGARYE NAEEDGISHF LEHMAFKGTK
     TRTAKQIAEA FDAIGGHFNA YTGHENTVYY ARVLSENCDK ALNILADIIQ NSIFSDEEIA
     KEYQVIMQEI AHHQDNPDDL VYEKFYNKVY REQPLGKSIL GTAKTLATFT KEHFFNFIDK
     YYNAANLYLS IAGNIDHDKI VIIAEQLFSS LKQGVKSSFI PAKYIGGNGF INKELEQTSL
     VLGFEGTSYI NLEKLYQTHL LSIIFGGGMS SRLFQSIREK LGLAYAVGSY NSAYFDSGVF
     TIYASTAHDK LELLYKEIKN EIIKMTEQVS TEEILRAKTQ LRSNLQMAQE KNTYKSEEIG
     KNYSVFGQYI SPEEIMEIIM SIKADDIINT ANKIFSGTTT SAIIGPNDLQ GF