RIP1_MYCS2
ID RIP1_MYCS2 Reviewed; 406 AA.
AC A0QVH8;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Zinc metalloprotease Rip1;
DE EC=3.4.24.-;
DE AltName: Full=Regulator of sigma KLM proteases;
DE AltName: Full=S2P endopeptidase;
DE AltName: Full=Site-2-type intramembrane protease;
DE AltName: Full=site-2 protease Rip1;
DE Short=S2P protease Rip1;
GN Name=rip1; OrderedLocusNames=MSMEG_2579, MSMEI_2517;
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 FUNCTION, ACTIVITY REGULATION, SUBSTRATE, AND 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 FUNCTION, SUBSTRATES, AND 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 -!- FUNCTION: A probable intramembrane site-2 protease (S2P) that cleaves
CC type-2 transmembrane proteins within their membrane-spanning domains.
CC Degrades PbpB (PBP3, FtsI) under conditions of oxidatives stress;
CC degradation is inhibited by Wag31-PbpB interaction. Also cleaves anti-
CC sigma factors RskA, RslA and RslM. Site-1 proteases have not yet been
CC identified in this organism.
CC -!- FUNCTION: Regulated intramembrane proteolysis (RIP) occurs when an
CC extracytoplasmic signal (possibly oxidative stress) triggers a
CC concerted proteolytic cascade to transmit information and elicit
CC cellular responses. The membrane-spanning regulatory substrate protein
CC (includes anti-sigma factors RskA, RslA, RsmA, and PbpB) is first cut
CC extracytoplasmically (site-1 protease, S1P), then within the membrane
CC itself (site-2 protease, S2P, this entry), while cytoplasmic proteases
CC finish degrading the regulatory protein, liberating the effector
CC protein (ECF sigma factors SigK, SigL and SigM).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Proteolysis is inhibited by Wag31; when Wag31 is
CC non-functional oxidative stress increases proteolysis.
CC {ECO:0000269|PubMed:19496931}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Not essential. No degradation of PbpB (PBP3,
CC FtsI) in the presence of mutant Wag31 upon H(2)O(2) exposure
CC (PubMed:19496931). Altered processing of anti-sigma factors RskA, RslA
CC and RslM (PubMed:20545848). {ECO:0000269|PubMed:19496931,
CC ECO:0000269|PubMed:20545848}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; CP000480; ABK74716.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38985.1; -; Genomic_DNA.
DR RefSeq; WP_003893934.1; NZ_SIJM01000029.1.
DR RefSeq; YP_886916.1; NC_008596.1.
DR AlphaFoldDB; A0QVH8; -.
DR SMR; A0QVH8; -.
DR STRING; 246196.MSMEI_2517; -.
DR PRIDE; A0QVH8; -.
DR EnsemblBacteria; ABK74716; ABK74716; MSMEG_2579.
DR EnsemblBacteria; AFP38985; AFP38985; MSMEI_2517.
DR GeneID; 66733989; -.
DR KEGG; msg:MSMEI_2517; -.
DR KEGG; msm:MSMEG_2579; -.
DR PATRIC; fig|246196.19.peg.2545; -.
DR eggNOG; COG0750; Bacteria.
DR OMA; QYMVGFG; -.
DR OrthoDB; 1395197at2; -.
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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
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 SUPFAM; SSF50156; SSF50156; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..406
FT /note="Zinc metalloprotease Rip1"
FT /id="PRO_0000422676"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 125..209
FT /note="PDZ"
FT ACT_SITE 22
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 42910 MW; DEB463D29FCB7EFC CRC64;
MMFGIGIVLF ALAILVSVAL HECGHMWVAR ATGMKVRRYF VGFGPTLWST RRANRLGSTE
YGIKAIPLGG FCDIAGMTSV DEIAPEDRPY AMYKQKVWKR VAVLFAGPAM NFVIGLVLIY
GIAIVWGLPN LHQPTTAIVG ETGCVAPQIT LEEMGECTGP GPAALAGIQA GDEIVKVGDT
EVKDFAGMAA AVRKLDGPTR IEFKRDGRVM DTVVDVTPTQ RFTSADASAP STVGAIGVSA
VPVQPPAQYN PITAVPATFA FTGDLAVELG KSLAKIPTKI GALVEAIGGG ERDKETPISV
VGASIIGGET VDAGLWVAFW FFLAQLNFVL GAINLVPLLP FDGGHIAVAT YEKIRNMIRS
ARGMVAAGPV NYLKLMPATY VVLAVVAGYM LLTVTADLVN PLSIFQ
