RIP2_MYCTE
ID RIP2_MYCTE Reviewed; 259 AA.
AC H8EVJ1;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Putative zinc metalloprotease Rip2;
GN Name=rip2; OrderedLocusNames=ERDMAN_0399;
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 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 -!- 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; BAL64215.1; -; Genomic_DNA.
DR RefSeq; WP_003900129.1; NZ_KK339487.1.
DR AlphaFoldDB; H8EVJ1; -.
DR EnsemblBacteria; BAL64215; BAL64215; ERDMAN_0399.
DR KEGG; mtn:ERDMAN_0399; -.
DR PATRIC; fig|652616.3.peg.403; -.
DR HOGENOM; CLU_066211_0_0_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:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06158; S2P-M50_like_1; 1.
DR InterPro; IPR044537; S2P-M50-like.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..259
FT /note="Putative zinc metalloprotease Rip2"
FT /id="PRO_0000422675"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 61
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 259 AA; 28164 MW; 60787663F4A3C218 CRC64;
MSETGQRESV RPSPIFLGLL GLTAVGGALA WLAGETVQPL AYAGVFVMVI AGWLVSLCLH
EFGHAFTAWR FGDHDVAVRG YLTLDPRRYS HPMLSLGLPM LFIALGGIGL PGAAVYVHTW
FMTTARRTLV SLAGPTVNLA LAMLLLAATR LLFDPIHAVL WAGVAFLAFL QLTALVLNLL
PIPGLDGYAA LEPHLRPETQ RALAPAKQFA LVFRLVLFLA PTLNGWFFGV VYWLFDLSGV
SHRLAAAGSV LARFWSIWF
