DEGS_HAEIN
ID DEGS_HAEIN Reviewed; 340 AA.
AC P44947;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine endoprotease DegS;
DE EC=3.4.21.107;
DE AltName: Full=Site-1 protease DegS;
DE Short=S1P protease DegS;
DE AltName: Full=Site-1-type intramembrane protease;
GN Name=degS; Synonyms=hhoB, htrH; OrderedLocusNames=HI_0945;
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-1 protease (S1P) that cleaves the peptide bond between
CC 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane
CC proteolysis (RIP) cascade. When heat shock or other environmental
CC stresses disrupt protein folding in the periplasm, DegS senses the
CC accumulation of unassembled outer membrane porins (OMP) and then
CC initiates RseA (anti sigma-E factor) degradation by cleaving its
CC periplasmic domain, making it a substrate for subsequent cleavage by
CC RseP. This cascade ultimately leads to the sigma-E-driven expression of
CC a variety of factors dealing with folding stress in the periplasm and
CC OMP assembly. Required for basal and stress-induced degradation of RseA
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC -!- ACTIVITY REGULATION: Allosterically activated by the C-terminus of
CC exposed OMP peptides (consensus Tyr-X-Phe-COOH); cleavage only occurs
CC in the presence of peptides. Inhibited when RseB is bound to RseA.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The PDZ domain probably binds peptides ending with C-terminal
CC Tyr-X-Phe sequences, which activates proteolysis. In the absence of OMP
CC peptides the PDZ domain inhibits peptidase activity (By similarity).
CC {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, this enzyme), then within the membrane itself (site-2
CC protease, S2P), while cytoplasmic proteases finish degrading the
CC regulatory protein, liberating the effector protein (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; L42023; AAC22599.1; -; Genomic_DNA.
DR PIR; I64103; I64103.
DR RefSeq; NP_439105.1; NC_000907.1.
DR RefSeq; WP_010869093.1; NC_000907.1.
DR AlphaFoldDB; P44947; -.
DR SMR; P44947; -.
DR STRING; 71421.HI_0945; -.
DR MEROPS; S01.275; -.
DR EnsemblBacteria; AAC22599; AAC22599; HI_0945.
DR KEGG; hin:HI_0945; -.
DR PATRIC; fig|71421.8.peg.986; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_2_2_6; -.
DR OMA; THGWVLE; -.
DR PhylomeDB; P44947; -.
DR BioCyc; HINF71421:G1GJ1-985-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011783; Pept_S1C_DegS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR TIGRFAMs; TIGR02038; protease_degS; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Serine endoprotease DegS"
FT /id="PRO_0000026939"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 5..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..340
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 251..323
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 92
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE4"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE4"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE4"
SQ SEQUENCE 340 AA; 36039 MW; 69EA452DF5A10649 CRC64;
MLKKLFHSAL WGLAAAGVIL FAVPRLNNSN IFTSDDIISF KNAVRIASPA VVNVYNRSFS
SASINDNDQL QVNNLGSGVI MSKDGYILTN KHLIQNADQI VVALQNGNIF EASLVGSDDL
TDLAVLKIRA DNLSTIPQNS ARQAHVGDVV LAIGNPYNLG QSVSQGIISA IGRNAVGDSV
GRQNFIQTDA SINRGNSGGA LINSAGELVG ISTLSIGKTA NEIAEGLNFA IPIDIANDVL
RKIMRDGRVI RGYFGVQSDI SSSSEEGIVI TDVSPNSPAA KSGIQVGDVI LKLNNQEGIS
AREMMQIIAN TKPNSKVLVT ILRLGKILQI PVVIEEFPVN
