RSEP_SALT1
ID RSEP_SALT1 Reviewed; 450 AA.
AC D0ZKX9;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Regulator of sigma-E 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; Synonyms=yaeL; OrderedLocusNames=STM14_0265;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19170886; DOI=10.1111/j.1365-2958.2009.06597.x;
RA Muller C., Bang I.S., Velayudhan J., Karlinsey J., Papenfort K., Vogel J.,
RA Fang F.C.;
RT "Acid stress activation of the sigma(E) stress response in Salmonella
RT enterica serovar Typhimurium.";
RL Mol. Microbiol. 71:1228-1238(2009).
CC -!- FUNCTION: A site-2 regulated intramembrane protease that cleaves the
CC 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. {ECO:0000269|PubMed:19170886}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: Deletion of the PDZ domains leads to dis-inhibition of protease
CC activity and almost complete loss of RseA even under non-inducing
CC conditions. {ECO:0000269|PubMed:19170886}.
CC -!- DISRUPTION PHENOTYPE: Not essential. Normal levels of sigma-E function
CC at pH 7.0, loss of acid stress induction of sigma-E. 100-fold decreased
CC survival in acidified murine macrophages.
CC {ECO:0000269|PubMed:19170886}.
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; CP001363; ACY86799.1; -; Genomic_DNA.
DR RefSeq; WP_000949017.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZKX9; -.
DR SMR; D0ZKX9; -.
DR EnsemblBacteria; ACY86799; ACY86799; STM14_0265.
DR KEGG; seo:STM14_0265; -.
DR PATRIC; fig|588858.6.peg.373; -.
DR HOGENOM; CLU_025778_0_2_6; -.
DR OMA; QYMVGFG; -.
DR BioCyc; SENT588858:STM14_RS01700-MON; -.
DR Proteomes; UP000002695; 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:0097533; P:cellular stress response to acid chemical; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
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; Repeat; Stress response; Transmembrane;
KW Transmembrane helix; Virulence; Zinc.
FT CHAIN 1..450
FT /note="Regulator of sigma-E protease RseP"
FT /id="PRO_0000424887"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..103
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..429
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
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..291
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 450 AA; 49184 MW; 50A748A774A70B7B CRC64;
MLSILWNLAA FIIALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR RTDRYGTEYV
IALIPLGGYV KMLDERAEPV APELRRHAFN NKTVGQRAAI IAAGPVANFI FAIFAYWLVF
IIGVPGVRPV IGEITPNSIA AQAQIAPGTE LKAVDGIETP DWDAVRLQLV SKIGDQQTTV
SVAPFGSDQR QDKTLDLRHW AFEPDKQDPV SSLGIRPRGP QIEPVLSEVQ ANSAASKAGL
QAGDRIVKVD GQPLTQWMKF VTFVRDNPGK PLALEIERQG SALSLTLTPD TKSVNGKAEG
FAGVVPKIIP LPEEYKTIRQ YGPFSAILEA TDKTWQLMKL TVSMLGKLIT GDVKLNNLSG
PISIAQGAGM SAEFGVIYYL MFLALISVNL GIINLFPLPV LDGGHLLFLA IEKLKGGPVS
ERVQDFSYRI GSILLVLLMG LALFNDFSRL
