ID   Y522_RICBR              Reviewed;         412 AA.
AC   Q1RJ61;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Uncharacterized zinc protease RBE_0522;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=RBE_0522;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04603.1; -; Genomic_DNA.
DR   RefSeq; WP_011477194.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJ61; -.
DR   SMR; Q1RJ61; -.
DR   STRING; 336407.RBE_0522; -.
DR   MEROPS; M16.016; -.
DR   EnsemblBacteria; ABE04603; ABE04603; RBE_0522.
DR   KEGG; rbe:RBE_0522; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_0_5; -.
DR   OMA; IDVVCDM; -.
DR   OrthoDB; 1188251at2; -.
DR   Proteomes; UP000001951; 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 RBE_0522"
FT                   /id="PRO_0000295169"
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;  46344 MW;  135975F0EB3B88D0 CRC64;
     MKENFNVSKL KNGLTILTYN MPYVNSVAIN LIAKVGSRYE NPGEEGIAHF LEHMAFKGTK
     TRTAKQIAEE FDSIGGHFNA YTGHEKTVYY SRVLSENCNK ALAIIADIVQ NSAFAEEEIA
     KEYQVILQEI AHAQDNPDDL VYEKFYNSVF KDQPLGKPIL GTSKTIETFN RDHFLKFTGK
     HYNAENFYLS IAGNVDHEEI VKEAERLFSS LTQGEKSNFS PAKYIGGHSF INKDLEQTTL
     ILGFEGTSYI NLERLYQTQL LAIIFGGGMS SRLFQHIREK LGLAYAVGSY NSPYFDSGVF
     TIYASTAHDK LELLAAELKN EIKRMAEQVK QEEIERARTQ IRSNLQMAQE KVAYKSEEIG
     KNYAVFGKYI SPEEIMEIIM NIKAADIIQT ANRIFSSSAT SAVIGPNNLS GF