RSEP_ECOLI
ID RSEP_ECOLI Reviewed; 450 AA.
AC P0AEH1; P37764;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=ecfE, yaeL; OrderedLocusNames=b0176, JW0171;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11274153; DOI=10.1074/jbc.m100464200;
RA Dartigalongue C., Missiakas D., Raina S.;
RT "Characterization of the Escherichia coli sigma E regulon.";
RL J. Biol. Chem. 276:20866-20875(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
RX PubMed=2995358; DOI=10.1016/s0021-9258(17)38988-3;
RA Icho T., Sparrow C.P., Raetz C.R.H.;
RT "Molecular cloning and sequencing of the gene for CDP-diglyceride
RT synthetase of Escherichia coli.";
RL J. Biol. Chem. 260:12078-12083(1985).
RN [7]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [8]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-22.
RX PubMed=11689431; DOI=10.1093/emboj/20.21.5908;
RA Dartigalongue C., Loferer H., Raina S.;
RT "EcfE, a new essential inner membrane protease: its role in the regulation
RT of heat shock response in Escherichia coli.";
RL EMBO J. 20:5908-5918(2001).
RN [9]
RP DISCUSSION OF FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF HIS-22; GLU-23; HIS-26; VAL-261 AND ASP-402.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11750129; DOI=10.1016/s0378-1119(01)00823-x;
RA Kanehara K., Akiyama Y., Ito K.;
RT "Characterization of the yaeL gene product and its S2P-protease motifs in
RT Escherichia coli.";
RL Gene 281:71-79(2001).
RN [10]
RP FUNCTION IN CLEAVAGE OF RSEA, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP HIS-22 AND ASP-402.
RC STRAIN=K12;
RX PubMed=12183368; DOI=10.1101/gad.1002302;
RA Kanehara K., Ito K., Akiyama Y.;
RT "YaeL (EcfE) activates the sigma(E) pathway of stress response through a
RT site-2 cleavage of anti-sigma(E), RseA.";
RL Genes Dev. 16:2147-2155(2002).
RN [11]
RP FUNCTION IN THE CLEAVAGE OF RSEA, POSSIBLE ACTIVE SITE, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-23.
RC STRAIN=K12;
RX PubMed=12183369; DOI=10.1101/gad.1008902;
RA Alba B.M., Leeds J.A., Onufryk C., Lu C.Z., Gross C.A.;
RT "DegS and YaeL participate sequentially in the cleavage of RseA to activate
RT the sigma(E)-dependent extracytoplasmic stress response.";
RL Genes Dev. 16:2156-2168(2002).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11867724; DOI=10.1073/pnas.052018199;
RA Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W.,
RA von Heijne G.;
RT "Rapid topology mapping of Escherichia coli inner-membrane proteins by
RT prediction and PhoA/GFP fusion analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002).
RN [13]
RP INTERACTION WITH RSEA, DOMAIN, AND MUTAGENESIS OF GLY-214; 234-ALA-ALA-235;
RP GLY-243; ASP-244 AND ILE-246.
RC STRAIN=K12 / AD16;
RX PubMed=14633997; DOI=10.1093/emboj/cdg602;
RA Kanehara K., Ito K., Akiyama Y.;
RT "YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a
RT Gln-rich region of RseA.";
RL EMBO J. 22:6389-6398(2003).
RN [14]
RP FUNCTION IN THE CLEAVAGE OF RSEA, AND MUTAGENESIS OF HIS-22.
RX PubMed=15496982; DOI=10.1038/sj.emboj.7600449;
RA Akiyama Y., Kanehara K., Ito K.;
RT "RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane
RT sequences.";
RL EMBO J. 23:4434-4442(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [16]
RP FUNCTION IN CLEAVAGE OF RSEA, INTERACTION WITH RSEA, SUBSTRATE RECOGNITION,
RP AND MUTAGENESIS OF HIS-22; GLU-23; ASN-389; ASN-394; PRO-397 AND PRO-399.
RC STRAIN=K12 / AD16;
RX PubMed=18268014; DOI=10.1074/jbc.m709984200;
RA Koide K., Ito K., Akiyama Y.;
RT "Substrate recognition and binding by RseP, an Escherichia coli
RT intramembrane protease.";
RL J. Biol. Chem. 283:9562-9570(2008).
RN [17]
RP FUNCTION IN CLEAVAGE OF SIGNAL PEPTIDES, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF HIS-22.
RC STRAIN=K12;
RX PubMed=21810987; DOI=10.1073/pnas.1108376108;
RA Saito A., Hizukuri Y., Matsuo E., Chiba S., Mori H., Nishimura O., Ito K.,
RA Akiyama Y.;
RT "Post-liberation cleavage of signal peptides is catalyzed by the site-2
RT protease (S2P) in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13740-13745(2011).
RN [18]
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ILE-215 AND ILE-304.
RC STRAIN=K12;
RX PubMed=23016873; DOI=10.1111/mmi.12053;
RA Hizukuri Y., Akiyama Y.;
RT "PDZ domains of RseP are not essential for sequential cleavage of RseA or
RT stress-induced sigma(E) activation in vivo.";
RL Mol. Microbiol. 86:1232-1245(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 127-221, X-RAY CRYSTALLOGRAPHY
RP (0.98 ANGSTROMS) OF 222-309, FUNCTION IN CLEAVAGE OF RSEA, DOMAIN, AND
RP MUTAGENESIS OF ALA-115; ILE-145; LEU-151; TRP-162; LEU-169; LEU-213 AND
RP GLY-214.
RC STRAIN=K12;
RX PubMed=18945679; DOI=10.1074/jbc.m806603200;
RA Inaba K., Suzuki M., Maegawa K., Akiyama S., Ito K., Akiyama Y.;
RT "A pair of circularly permutated PDZ domains control RseP, the S2P family
RT intramembrane protease of Escherichia coli.";
RL J. Biol. Chem. 283:35042-35052(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 127-220, X-RAY CRYSTALLOGRAPHY
RP (1.60 ANGSTROMS) OF 222-307, DOMAIN, AND MUTAGENESIS OF ILE-215 AND
RP ILE-304.
RX PubMed=19706448; DOI=10.1073/pnas.0903289106;
RA Li X., Wang B., Feng L., Kang H., Qi Y., Wang J., Shi Y.;
RT "Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino
RT acid following DegS cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14837-14842(2009).
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, residue 'Val-148' of RseA may be required for this. This provides
CC the cell with sigma-E (RpoE) activity through the proteolysis of RseA.
CC Can also cleave sequences in transmembrane regions of other proteins
CC (such as LacY) as well as liberated signal peptides of beta-lactamase,
CC OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the
CC membrane. {ECO:0000269|PubMed:12183368, ECO:0000269|PubMed:12183369,
CC ECO:0000269|PubMed:15496982, ECO:0000269|PubMed:18268014,
CC ECO:0000269|PubMed:18945679, ECO:0000269|PubMed:21810987}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+) chelator 1,10-phenanthroline.
CC {ECO:0000269|PubMed:21810987}.
CC -!- SUBUNIT: Interacts with RseA; the third transmembrane domain can be
CC cross-linked to the transmembrane domain of RseA.
CC {ECO:0000269|PubMed:14633997, ECO:0000269|PubMed:18268014}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11689431,
CC ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:11867724,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11689431, ECO:0000269|PubMed:11750129,
CC ECO:0000269|PubMed:11867724, ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Part of the sigma-E regulon. Also has a primary sigma-70
CC factor promoter. {ECO:0000269|PubMed:11274153}.
CC -!- DOMAIN: The 2 circularly premutated PDZ domains act to negatively
CC regulate protease action on intact RseA; mutations in PDZ 1 (PDZ-N)
CC have a more deleterious effect than similar mutations in PDZ 2 (PDZ-C).
CC A 31 residue insertion in PDZ-C (between Val-261 and Met-262) domain
CC inhibits protease activity, whereas deletion of residues 203-279
CC alleviates the PDZ-inhibition, allowing cleavage of intact RseA.
CC {ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:14633997,
CC ECO:0000269|PubMed:18945679, ECO:0000269|PubMed:19706448,
CC ECO:0000269|PubMed:23016873}.
CC -!- DISRUPTION PHENOTYPE: Essential. Depletion experiments lead to
CC cessation of growth, elongated cells and limited lysis, as well as
CC decreased amounts of sigma-E. Not essential in an rseA deletion strain,
CC when sigma-E is overexpressed or in ompA-ompC deletion strain. In the
CC latter has severely decreased growth at 20 degrees Celsius.
CC Accumulation of an RseA proteolysis intermediate.
CC {ECO:0000269|PubMed:11274153, ECO:0000269|PubMed:11689431,
CC ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:12183368,
CC ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:23016873}.
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.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a negative regulator of sigma-E
CC function and to act directly on sigma-E and RpoH; this may not be
CC physiologically relevant. {ECO:0000305|PubMed:11689431}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF407012; AAL01378.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08605.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73287.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77851.1; -; Genomic_DNA.
DR EMBL; M11330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H64741; H64741.
DR RefSeq; NP_414718.1; NC_000913.3.
DR RefSeq; WP_001295561.1; NZ_STEB01000032.1.
DR PDB; 2ZPL; X-ray; 1.70 A; A/B/C=127-221.
DR PDB; 2ZPM; X-ray; 0.98 A; A=222-309.
DR PDB; 3ID1; X-ray; 1.67 A; A=127-220.
DR PDB; 3ID2; X-ray; 3.09 A; A/B=222-309.
DR PDB; 3ID3; X-ray; 2.01 A; A/B=222-309.
DR PDB; 3ID4; X-ray; 1.60 A; A=222-307.
DR PDBsum; 2ZPL; -.
DR PDBsum; 2ZPM; -.
DR PDBsum; 3ID1; -.
DR PDBsum; 3ID2; -.
DR PDBsum; 3ID3; -.
DR PDBsum; 3ID4; -.
DR AlphaFoldDB; P0AEH1; -.
DR SMR; P0AEH1; -.
DR BioGRID; 4261736; 104.
DR DIP; DIP-48061N; -.
DR IntAct; P0AEH1; 2.
DR STRING; 511145.b0176; -.
DR MEROPS; M50.004; -.
DR TCDB; 9.B.149.2.3; the m50 peptidase (m50-p) family.
DR jPOST; P0AEH1; -.
DR PaxDb; P0AEH1; -.
DR PRIDE; P0AEH1; -.
DR EnsemblBacteria; AAC73287; AAC73287; b0176.
DR EnsemblBacteria; BAA77851; BAA77851; BAA77851.
DR GeneID; 66671536; -.
DR GeneID; 944871; -.
DR KEGG; ecj:JW0171; -.
DR KEGG; eco:b0176; -.
DR PATRIC; fig|1411691.4.peg.2103; -.
DR EchoBASE; EB2331; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_2_6; -.
DR InParanoid; P0AEH1; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; P0AEH1; -.
DR BioCyc; EcoCyc:EG12436-MON; -.
DR BioCyc; MetaCyc:EG12436-MON; -.
DR EvolutionaryTrace; P0AEH1; -.
DR PRO; PR:P0AEH1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0043856; F:anti-sigma factor antagonist activity; IMP:EcoCyc.
DR GO; GO:0045152; F:antisigma factor binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..450
FT /note="Regulator of sigma-E protease RseP"
FT /id="PRO_0000088417"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..103
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11750129"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11750129"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..429
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11750129"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 127..220
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 222..309
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 23
FT /evidence="ECO:0000305"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT MUTAGEN 22
FT /note="H->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:11689431,
FT ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:12183368,
FT ECO:0000269|PubMed:15496982, ECO:0000269|PubMed:18268014,
FT ECO:0000269|PubMed:21810987"
FT MUTAGEN 22
FT /note="H->F: Loss of protease activity of RseA and signal
FT peptides, does not complement deletion mutant. Binds
FT substrate."
FT /evidence="ECO:0000269|PubMed:11689431,
FT ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:12183368,
FT ECO:0000269|PubMed:15496982, ECO:0000269|PubMed:18268014,
FT ECO:0000269|PubMed:21810987"
FT MUTAGEN 23
FT /note="E->A: Low basal sigma-E activity, sigma-E not
FT induced. No proteolysis of RseA."
FT /evidence="ECO:0000269|PubMed:11750129,
FT ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:18268014"
FT MUTAGEN 23
FT /note="E->D: Behaves like wild-type in vivo, slight
FT reduction in RseA cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:11750129,
FT ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:18268014"
FT MUTAGEN 23
FT /note="E->Q: Does not complement deletion mutant."
FT /evidence="ECO:0000269|PubMed:11750129,
FT ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:18268014"
FT MUTAGEN 23
FT /note="E->S: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:11750129,
FT ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:18268014"
FT MUTAGEN 26
FT /note="H->F: Does not complement deletion mutant."
FT /evidence="ECO:0000269|PubMed:11750129"
FT MUTAGEN 115
FT /note="A->V: No effect. Cleaves RseA without previous DegS
FT cleavage; when associated with R-214."
FT /evidence="ECO:0000269|PubMed:18945679"
FT MUTAGEN 145
FT /note="I->N: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:18945679"
FT MUTAGEN 151
FT /note="L->P: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:18945679"
FT MUTAGEN 162
FT /note="W->R: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:18945679"
FT MUTAGEN 169
FT /note="L->S: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:18945679"
FT MUTAGEN 213
FT /note="L->P: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:18945679"
FT MUTAGEN 214
FT /note="G->E,Q: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:14633997,
FT ECO:0000269|PubMed:18945679"
FT MUTAGEN 214
FT /note="G->R: Weakly cuts RseA without previous DegS
FT cleavage. Stronger cleavage; when associated with V-115."
FT /evidence="ECO:0000269|PubMed:14633997,
FT ECO:0000269|PubMed:18945679"
FT MUTAGEN 215
FT /note="I->A: No cleavage of RseA in vitro
FT (PubMed:19706448), cleavage of RseA (PubMed:23016873) in
FT vivo."
FT /evidence="ECO:0000269|PubMed:19706448,
FT ECO:0000269|PubMed:23016873"
FT MUTAGEN 234..235
FT /note="AA->KK: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:14633997"
FT MUTAGEN 243
FT /note="G->Q: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:14633997"
FT MUTAGEN 244
FT /note="D->K: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:14633997"
FT MUTAGEN 246
FT /note="I->Y: Cuts RseA without previous DegS cleavage."
FT /evidence="ECO:0000269|PubMed:14633997"
FT MUTAGEN 261
FT /note="V->VTDSYTQVASWTEPFPFSIQGDPRSDQETAFV: Does not
FT complement deletion mutant."
FT /evidence="ECO:0000269|PubMed:11750129"
FT MUTAGEN 304
FT /note="I->A: No cleavage of RseA in vitro
FT (PubMed:19706448), cleavage of RseA (PubMed:23016873) in
FT vivo."
FT /evidence="ECO:0000269|PubMed:19706448,
FT ECO:0000269|PubMed:23016873"
FT MUTAGEN 389
FT /note="N->C,G,L: Decreased substrate binding, retains some
FT proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18268014"
FT MUTAGEN 389
FT /note="N->Q: No effect."
FT /evidence="ECO:0000269|PubMed:18268014"
FT MUTAGEN 394
FT /note="N->C: Decreased substrate binding, retains some
FT proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18268014"
FT MUTAGEN 397
FT /note="P->C: Decreased substrate binding, retains some
FT proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18268014"
FT MUTAGEN 399
FT /note="P->C: Decreased substrate binding, retains some
FT proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18268014"
FT MUTAGEN 402
FT /note="D->N: Does not complement deletion mutant, loss of
FT protease activity."
FT /evidence="ECO:0000269|PubMed:11750129,
FT ECO:0000269|PubMed:12183368"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3ID1"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:3ID1"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3ID1"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:3ID1"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3ID1"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:3ID1"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:3ID1"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3ID1"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3ID1"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3ID1"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2ZPM"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3ID2"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2ZPM"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2ZPM"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:2ZPM"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:2ZPM"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:2ZPM"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2ZPM"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3ID4"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:2ZPM"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:3ID4"
SQ SEQUENCE 450 AA; 49071 MW; 81A93BC113FBB66C CRC64;
MLSFLWDLAS FIVALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR RTDKLGTEYV
IALIPLGGYV KMLDERAEPV VPELRHHAFN NKSVGQRAAI IAAGPVANFI FAIFAYWLVF
IIGVPGVRPV VGEIAANSIA AEAQIAPGTE LKAVDGIETP DWDAVRLQLV DKIGDESTTI
TVAPFGSDQR RDVKLDLRHW AFEPDKEDPV SSLGIRPRGP QIEPVLENVQ PNSAASKAGL
QAGDRIVKVD GQPLTQWVTF VMLVRDNPGK SLALEIERQG SPLSLTLIPE SKPGNGKAIG
FVGIEPKVIP LPDEYKVVRQ YGPFNAIVEA TDKTWQLMKL TVSMLGKLIT GDVKLNNLSG
PISIAKGAGM TAELGVVYYL PFLALISVNL GIINLFPLPV LDGGHLLFLA IEKIKGGPVS
ERVQDFCYRI GSILLVLLMG LALFNDFSRL
