RSEP_YERPE
ID RSEP_YERPE Reviewed; 451 AA.
AC Q8ZH59; Q0WHZ4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protease RseP;
DE EC=3.4.24.-;
DE AltName: Full=S2P endopeptidase;
DE AltName: Full=Site-2 protease RseP;
DE Short=S2P protease RseP;
DE AltName: Full=Site-2-type intramembrane protease;
GN Name=rseP; OrderedLocusNames=YPO1051, y3128, YP_2799;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves
CC the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane
CC region of RseA. Part of a regulated intramembrane proteolysis (RIP)
CC cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of
CC RseA. This provides the cell with sigma-E (RpoE) activity through the
CC proteolysis of RseA (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with RseA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The 2 circularly premutated PDZ domains act to negatively
CC regulate protease action on intact RseA. {ECO:0000250}.
CC -!- MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs when an
CC extracytoplasmic signal triggers a concerted proteolytic cascade to
CC transmit information and elicit cellular responses. A membrane-spanning
CC regulatory substrate protein is first cut extracytoplasmically (site-1
CC protease, S1P), then within the membrane itself (site-2 protease, S2P,
CC this enzyme), while cytoplasmic proteases finish degrading the
CC regulatory protein, liberating the effector protein (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AL590842; CAL19716.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86678.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62983.1; -; Genomic_DNA.
DR PIR; AB0129; AB0129.
DR RefSeq; WP_002212138.1; NZ_WUCM01000044.1.
DR RefSeq; YP_002346094.1; NC_003143.1.
DR AlphaFoldDB; Q8ZH59; -.
DR SMR; Q8ZH59; -.
DR STRING; 214092.YPO1051; -.
DR MEROPS; M50.004; -.
DR PaxDb; Q8ZH59; -.
DR DNASU; 1148075; -.
DR EnsemblBacteria; AAM86678; AAM86678; y3128.
DR EnsemblBacteria; AAS62983; AAS62983; YP_2799.
DR GeneID; 66844575; -.
DR KEGG; ype:YPO1051; -.
DR KEGG; ypk:y3128; -.
DR KEGG; ypm:YP_2799; -.
DR PATRIC; fig|214092.21.peg.1339; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_2_6; -.
DR OMA; QYMVGFG; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; -; 2.
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; 2.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..451
FT /note="Protease RseP"
FT /id="PRO_0000088422"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 115..186
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 199..280
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 451 AA; 49429 MW; 9EBE92728D25B8A8 CRC64;
MMSILWSLAA FIVALGILIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR RTDRQGTEYV
IALIPLGGYV KMLDERVEAV APELRHQSFN NKTVLQRAAI VSAGPIANFL FAIVAYWLVF
IIGVPSVRPV IGDISPQSIA AQANISSGME LKSVDGIETP DWDSVRLALI SRIGDKQMQV
GVAPFGSDNV VEKTLDLRQW QFEPDKQDPV VALGIIPRGP QIESVLAEVQ PGSAAQKAGL
QAGDRIVKVN GQLLDRWQTF VLQVRDNPGQ PLVLDIERES TPLSLTLIPD TKSVGENRSE
GFAGVVPKVI PLPDEYKTIR QYGPFTAVYQ AGDKTWQLMR LTVSMLGKLI TGDVKLNNLS
GPISIAQGAG LSAEYGLVYY LMFLALISVN LGIINLFPLP VLDGGHLLFL AIEKLKGGPV
SERVQDFSYR IGSILLVLLM GLALFNDFSR L
