RSEP_HAEIN
ID RSEP_HAEIN Reviewed; 443 AA.
AC P44936;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Regulator of sigma E protease;
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=HI_0918;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves
CC a peptide bond in the transmembrane region of RseA. Part of a regulated
CC intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to
CC release the cytoplasmic domain of RseA. This provides the cell with
CC sigma-E (RpoE) activity through the proteolysis of RseA (By
CC 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; L42023; AAC22576.1; -; Genomic_DNA.
DR PIR; D64161; D64161.
DR RefSeq; NP_439078.1; NC_000907.1.
DR RefSeq; WP_005693265.1; NC_000907.1.
DR AlphaFoldDB; P44936; -.
DR SMR; P44936; -.
DR STRING; 71421.HI_0918; -.
DR EnsemblBacteria; AAC22576; AAC22576; HI_0918.
DR KEGG; hin:HI_0918; -.
DR PATRIC; fig|71421.8.peg.959; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_2_6; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; P44936; -.
DR BioCyc; HINF71421:G1GJ1-957-MON; -.
DR Proteomes; UP000000579; 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; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 2.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR TIGRFAMs; TIGR00054; TIGR00054; 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..443
FT /note="Regulator of sigma E protease"
FT /id="PRO_0000088442"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 106..185
FT /note="PDZ 1"
FT DOMAIN 198..287
FT /note="PDZ 2"
FT ACT_SITE 22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 443 AA; 49070 MW; A4C98A2AD2B6BBBE CRC64;
MSFLWSLGSF IIAIAVLVSV HEYGHFWAAR KCGIKVHRFS IGFGKVIWKR IDKYGTEFAV
SMIPLGGYVK MLDGRNEVVP AEQKSQAFDS KSVLQRSFVI IAGPLANFIF AIFAYWVIYL
YGMPTVKPVI ESITPNSIAA QAHIEPNTQI LTIDGEETQD WETINMLLAT KMGEPNVEIS
LSPFNSNIEQ QRTLNLTNWT FDPEKESAFE ALGIMPMRPK IEMVLSKVVQ NSPAEKAGLQ
IGDKILKENL TALPWQDFIK QVEQGESFSI KVERNGETFD KVLTPVRNQN GKWFVGVSPA
LTKLADEYRT ELKYGILESL QKGIEKTGQL SLLTLKILGK LLTGDLSLNN LSGPISIAKG
AGASANIGLV YFLSFMALIS VNLGIMNLFP LPVLDGGHLV FLTMEAVKGK PVSERVQSIC
YRIGAALLLS LTVFALFNDF LRL
