ID   Y203_RICCN              Reviewed;         358 AA.
AC   Q92J66;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative zinc metalloprotease RC0203;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=RC0203;
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: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; AE006914; AAL02741.1; -; Genomic_DNA.
DR   PIR; C97725; C97725.
DR   RefSeq; WP_010976870.1; NC_003103.1.
DR   AlphaFoldDB; Q92J66; -.
DR   EnsemblBacteria; AAL02741; AAL02741; RC0203.
DR   KEGG; rco:RC0203; -.
DR   PATRIC; fig|272944.4.peg.233; -.
DR   HOGENOM; CLU_025778_1_0_5; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000000816; 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; -; 1.
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; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..358
FT                   /note="Putative zinc metalloprotease RC0203"
FT                   /id="PRO_0000088457"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          102..186
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  39375 MW;  165C9CC5FCED317A CRC64;
     MLSIIGFIIT ISILVFIHEF GHYCIARYFN VKVEEFSIGF GKALIGITDK KGVRWKICLI
     PLGGYVKIYG YDRSLMDKTK EVNEKVAFDA KSCLERFLIV AAGPLINYLL AIIIFAGFYC
     YFGKTEIPPI IGNVVASSPA ERADLRAGDK IVKVNDKSVK DFGDVQREIL INGFSSSTLT
     IERKSEEFIV NIMPQEIIIS PPEEKQVNKK TLRIGIIAKN ESIHTKIGIL GGLWEAINTT
     IDMSALTLNA ISQMIVGKRS FDEIGGPIAI AKESGKSIAG GTQMYLLFIA MLSVNLGLLN
     LLPIPVLDGG HLVFILYEAI TGKLPHPKTK NILLQLGAII IIFLIIIAVS NDIQNLFS