ID   Y161_RICPR              Reviewed;         359 AA.
AC   Q9ZE02;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Putative zinc metalloprotease RP161;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=RP161;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14628.1; -; Genomic_DNA.
DR   PIR; E71726; E71726.
DR   RefSeq; NP_220551.1; NC_000963.1.
DR   RefSeq; WP_004595877.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE02; -.
DR   STRING; 272947.RP161; -.
DR   EnsemblBacteria; CAA14628; CAA14628; CAA14628.
DR   GeneID; 57569290; -.
DR   KEGG; rpr:RP161; -.
DR   PATRIC; fig|272947.5.peg.165; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_5; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000002480; 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; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..359
FT                   /note="Putative zinc metalloprotease RP161"
FT                   /id="PRO_0000088458"
FT   TRANSMEM        101..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          104..188
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   359 AA;  39744 MW;  41EF8E4DBD955364 CRC64;
     MLSLIGFIIT ISILVFIHEF GHYCIARYLD VKVEEFSIGF GKELIGITDR KGVRWKLCFI
     PLGGYVKIYG YDSSTRIIDK TKEVNEEVTF YSRSCLARFS IVAAGPLINY LLAVIIFTSF
     YCYFGKVEIP PIIGDVVAAS PAERAGLKEG DKIVKVNNKY VKDFVDVQKE ILINGFSSST
     LTIARKSEEF KVNIRPQEII ISHPEKKKIG KTFRIGIIAK NEPIHTKIGI FGGVLEAINT
     TIDISTLTLK AISQMILGTR PLDEIGGPIS IAQESGKSMA SGAQMYLLFI AMLSINLGLL
     NLLPIPVLDG GHLIFILYEA ITGRLPNPKT RNILLQLGAV IILLLIIISI SNDIKNLFY