RIP2_MYCS2
ID RIP2_MYCS2 Reviewed; 259 AA.
AC A0QQH5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Putative zinc metalloprotease Rip2;
DE EC=3.4.24.-;
GN Name=rip2; OrderedLocusNames=MSMEG_0756, MSMEI_0741;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=19496931; DOI=10.1111/j.1365-2958.2009.06750.x;
RA Mukherjee P., Sureka K., Datta P., Hossain T., Barik S., Das K.P.,
RA Kundu M., Basu J.;
RT "Novel role of Wag31 in protection of mycobacteria under oxidative
RT stress.";
RL Mol. Microbiol. 73:103-119(2009).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
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 degradation of PbpB
CC (PBP3, FtsI) upon depletion experiments (PubMed:19496931). No effect on
CC processing of anti-sigma factors RskA, RslA and RsmA (PubMed:20545848).
CC {ECO:0000269|PubMed:19496931, ECO:0000269|PubMed:20545848}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK74514.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37221.1; -; Genomic_DNA.
DR RefSeq; WP_011727171.1; NZ_SIJM01000036.1.
DR RefSeq; YP_885163.1; NC_008596.1.
DR AlphaFoldDB; A0QQH5; -.
DR STRING; 246196.MSMEI_0741; -.
DR EnsemblBacteria; ABK74514; ABK74514; MSMEG_0756.
DR EnsemblBacteria; AFP37221; AFP37221; MSMEI_0741.
DR GeneID; 66738932; -.
DR KEGG; msg:MSMEI_0741; -.
DR KEGG; msm:MSMEG_0756; -.
DR PATRIC; fig|246196.19.peg.753; -.
DR eggNOG; COG1994; Bacteria.
DR OMA; HEIMHGL; -.
DR OrthoDB; 1401629at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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; Reference proteome; Transmembrane; Transmembrane helix;
KW Virulence; Zinc.
FT CHAIN 1..259
FT /note="Putative zinc metalloprotease Rip2"
FT /id="PRO_0000422677"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
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; 28371 MW; 13F5DDAFA3D2342F CRC64;
MNIRPLRQSV RPSPIFLLVI AVTAAGGALA WIAADTIRPL SYVGVFILVI AGWLMSLCLH
EFGHAFTAWR FGDHGVETRG YLTLNPLKYT HPMLSLGLPV LIIALGGIGF PGGAVYLQTH
WMTARQKSIV SLAGPAANLV LAVLLLGLTR AFWDPAHAVF WSGIAFLGFL QVTALVLNLL
PIPGLDGYGA LEPHLNPETQ RALAPAKQWG FLIVVVLLIT PALNRWFFEL VYWFFDFSGV
SSYLVSAGGQ LTRFWSAWF
