ID   RIP3_MYCTE              Reviewed;         393 AA.
AC   H8EUF2;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Putative zinc metalloprotease Rip3;
GN   Name=rip3; OrderedLocusNames=ERDMAN_2885;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   INDUCTION BY CARBON MONOXIDE (CO).
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA   Shiloh M.U., Manzanillo P., Cox J.S.;
RT   "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT   macrophage infection.";
RL   Cell Host Microbe 3:323-330(2008).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA   Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT   "M. tuberculosis intramembrane protease Rip1 controls transcription through
RT   three anti-sigma factor substrates.";
RL   Mol. Microbiol. 77:605-617(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC       carbon monoxide (CO). It is hoped that this regulon will give insight
CC       into the latent, or dormant phase of infection.
CC       {ECO:0000269|PubMed:18474359}.
CC   -!- DISRUPTION PHENOTYPE: Not essential. No effect on processing of anti-
CC       sigma factors RsdA, RskA, RslA or RsmA. {ECO:0000269|PubMed:20545848}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AP012340; BAL66669.1; -; Genomic_DNA.
DR   RefSeq; WP_003899401.1; NZ_KK339487.1.
DR   AlphaFoldDB; H8EUF2; -.
DR   SMR; H8EUF2; -.
DR   EnsemblBacteria; BAL66669; BAL66669; ERDMAN_2885.
DR   KEGG; mtn:ERDMAN_2885; -.
DR   PATRIC; fig|652616.3.peg.2938; -.
DR   HOGENOM; CLU_037123_1_2_11; -.
DR   Proteomes; UP000007568; 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; 3.10.580.10; -; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR008915; Peptidase_M50.
DR   InterPro; IPR016483; UCP006404_Pept_M50_CBS.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF02163; Peptidase_M50; 2.
DR   PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   CBS domain; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Repeat; Transmembrane; Transmembrane helix;
KW   Zinc.
FT   CHAIN           1..393
FT                   /note="Putative zinc metalloprotease Rip3"
FT                   /id="PRO_0000422689"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          251..308
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          315..376
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   393 AA;  41480 MW;  6790E021215B6F98 CRC64;
     MRDAIPLGRI AGFVVNVHWS VLVILWLFTW SLATMLPGTV GGYPAVVYWL LGAGGAVMLL
     ASLLAHELAH AVVARRAGVS VESVTLWLFG GVTALGGEAK TPKAAFRIAF AGPATSLALS
     ATFGALAITL AGVRTPAIVI SVAWWLATVN LLLGLFNLLP GAPLDGGRLV RAYLWRRHGD
     SVRAGIGAAR AGRVVALVLI ALGLAEFVAG GLVGGVWLAF IGWFIFAAAR EEETRISTQQ
     LFAGVRVADA MTAQPHTAPG WINVEDFIQR YVLGERHSAY PVADRDGSIT GLVALRQLRD
     VAPSRRSTTS VGDIALPLHS VPTARPQEPL TALLERMAPL GPRSRALVTE GSAVVGIVTP
     SDVARLIDVY RLAQPEPTFT TSPQDADRFS DAG