GENTAUR Molecular Products.

 RSEP_ECOLI              Reviewed;         450 AA.
 P0AEH1; P37764;
 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
 06-DEC-2005, sequence version 1.
 30-AUG-2017, entry version 107.
 RecName: Full=Regulator of sigma-E protease RseP;
          EC=3.4.24.-;
 AltName: Full=S2P endopeptidase;
 AltName: Full=Site-2 protease RseP;
          Short=S2P protease RseP;
 AltName: Full=Site-2-type intramembrane protease;
 Name=rseP; Synonyms=ecfE, yaeL; OrderedLocusNames=b0176, JW0171;
 Escherichia coli (strain K12).
 Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
 Enterobacteriaceae; Escherichia.
 NCBI_TaxID=83333;
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION
 PHENOTYPE.
 PubMed=11274153; DOI=10.1074/jbc.M100464200;
 Dartigalongue C., Missiakas D., Raina S.;
 "Characterization of the Escherichia coli sigma E regulon.";
 J. Biol. Chem. 276:20866-20875(2001).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
 Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
 Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
 Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
 "Systematic sequencing of the Escherichia coli genome: analysis of the
 4.0 - 6.0 min (189,987 - 281,416bp) region.";
 Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=K12 / MG1655 / ATCC 47076;
 Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
 Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
 Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
 "Sequence of minutes 4-25 of Escherichia coli.";
 Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=K12 / MG1655 / ATCC 47076;
 PubMed=9278503; DOI=10.1126/science.277.5331.1453;
 Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
 Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
 Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
 Mau B., Shao Y.;
 "The complete genome sequence of Escherichia coli K-12.";
 Science 277:1453-1462(1997).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
 PubMed=16738553; DOI=10.1038/msb4100049;
 Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
 Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
 "Highly accurate genome sequences of Escherichia coli K-12 strains
 MG1655 and W3110.";
 Mol. Syst. Biol. 2:E1-E5(2006).
 [6]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
 PubMed=2995358;
 Icho T., Sparrow C.P., Raetz C.R.H.;
 "Molecular cloning and sequencing of the gene for CDP-diglyceride
 synthetase of Escherichia coli.";
 J. Biol. Chem. 260:12078-12083(1985).
 [7]
 IDENTIFICATION.
 PubMed=7984428; DOI=10.1093/nar/22.22.4756;
 Borodovsky M., Rudd K.E., Koonin E.V.;
 "Intrinsic and extrinsic approaches for detecting genes in a bacterial
 genome.";
 Nucleic Acids Res. 22:4756-4767(1994).
 [8]
 SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-22.
 PubMed=11689431; DOI=10.1093/emboj/20.21.5908;
 Dartigalongue C., Loferer H., Raina S.;
 "EcfE, a new essential inner membrane protease: its role in the
 regulation of heat shock response in Escherichia coli.";
 EMBO J. 20:5908-5918(2001).
 [9]
 DISCUSSION OF FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN,
 DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-22; GLU-23; HIS-26;
 VAL-261 AND ASP-402.
 STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
 PubMed=11750129; DOI=10.1016/S0378-1119(01)00823-X;
 Kanehara K., Akiyama Y., Ito K.;
 "Characterization of the yaeL gene product and its S2P-protease motifs
 in Escherichia coli.";
 Gene 281:71-79(2001).
 [10]
 FUNCTION IN CLEAVAGE OF RSEA, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
 HIS-22 AND ASP-402.
 STRAIN=K12;
 PubMed=12183368; DOI=10.1101/gad.1002302;
 Kanehara K., Ito K., Akiyama Y.;
 "YaeL (EcfE) activates the sigma(E) pathway of stress response through
 a site-2 cleavage of anti-sigma(E), RseA.";
 Genes Dev. 16:2147-2155(2002).
 [11]
 FUNCTION IN THE CLEAVAGE OF RSEA, POSSIBLE ACTIVE SITE, DISRUPTION
 PHENOTYPE, AND MUTAGENESIS OF GLU-23.
 STRAIN=K12;
 PubMed=12183369; DOI=10.1101/gad.1008902;
 Alba B.M., Leeds J.A., Onufryk C., Lu C.Z., Gross C.A.;
 "DegS and YaeL participate sequentially in the cleavage of RseA to
 activate the sigma(E)-dependent extracytoplasmic stress response.";
 Genes Dev. 16:2156-2168(2002).
 [12]
 SUBCELLULAR LOCATION.
 STRAIN=K12 / JM109 / ATCC 53323;
 PubMed=11867724; DOI=10.1073/pnas.052018199;
 Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N.,
 de Gier J.-W., von Heijne G.;
 "Rapid topology mapping of Escherichia coli inner-membrane proteins by
 prediction and PhoA/GFP fusion analysis.";
 Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002).
 [13]
 INTERACTION WITH RSEA, DOMAIN, AND MUTAGENESIS OF GLY-214;
 234-ALA-ALA-235; GLY-243; ASP-244 AND ILE-246.
 STRAIN=K12 / AD16;
 PubMed=14633997; DOI=10.1093/emboj/cdg602;
 Kanehara K., Ito K., Akiyama Y.;
 "YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and
 a Gln-rich region of RseA.";
 EMBO J. 22:6389-6398(2003).
 [14]
 FUNCTION IN THE CLEAVAGE OF RSEA, AND MUTAGENESIS OF HIS-22.
 PubMed=15496982; DOI=10.1038/sj.emboj.7600449;
 Akiyama Y., Kanehara K., Ito K.;
 "RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane
 sequences.";
 EMBO J. 23:4434-4442(2004).
 [15]
 SUBCELLULAR LOCATION.
 STRAIN=K12 / MG1655 / ATCC 47076;
 PubMed=15919996; DOI=10.1126/science.1109730;
 Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
 "Global topology analysis of the Escherichia coli inner membrane
 proteome.";
 Science 308:1321-1323(2005).
 [16]
 FUNCTION IN CLEAVAGE OF RSEA, INTERACTION WITH RSEA, SUBSTRATE
 RECOGNITION, AND MUTAGENESIS OF HIS-22; GLU-23; ASN-389; ASN-394;
 PRO-397 AND PRO-399.
 STRAIN=K12 / AD16;
 PubMed=18268014; DOI=10.1074/jbc.M709984200;
 Koide K., Ito K., Akiyama Y.;
 "Substrate recognition and binding by RseP, an Escherichia coli
 intramembrane protease.";
 J. Biol. Chem. 283:9562-9570(2008).
 [17]
 FUNCTION IN CLEAVAGE OF SIGNAL PEPTIDES, ENZYME REGULATION, AND
 MUTAGENESIS OF HIS-22.
 STRAIN=K12;
 PubMed=21810987; DOI=10.1073/pnas.1108376108;
 Saito A., Hizukuri Y., Matsuo E., Chiba S., Mori H., Nishimura O.,
 Ito K., Akiyama Y.;
 "Post-liberation cleavage of signal peptides is catalyzed by the site-
 2 protease (S2P) in bacteria.";
 Proc. Natl. Acad. Sci. U.S.A. 108:13740-13745(2011).
 [18]
 DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ILE-215 AND ILE-304.
 STRAIN=K12;
 PubMed=23016873; DOI=10.1111/mmi.12053;
 Hizukuri Y., Akiyama Y.;
 "PDZ domains of RseP are not essential for sequential cleavage of RseA
 or stress-induced sigma(E) activation in vivo.";
 Mol. Microbiol. 86:1232-1245(2012).
 [19]
 X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 127-221, X-RAY
 CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 222-309, FUNCTION IN CLEAVAGE OF
 RSEA, DOMAIN, AND MUTAGENESIS OF ALA-115; ILE-145; LEU-151; TRP-162;
 LEU-169; LEU-213 AND GLY-214.
 STRAIN=K12;
 PubMed=18945679; DOI=10.1074/jbc.M806603200;
 Inaba K., Suzuki M., Maegawa K., Akiyama S., Ito K., Akiyama Y.;
 "A pair of circularly permutated PDZ domains control RseP, the S2P
 family intramembrane protease of Escherichia coli.";
 J. Biol. Chem. 283:35042-35052(2008).
 [20]
 X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 127-220, X-RAY
 CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 222-307, DOMAIN, AND MUTAGENESIS
 OF ILE-215 AND ILE-304.
 PubMed=19706448; DOI=10.1073/pnas.0903289106;
 Li X., Wang B., Feng L., Kang H., Qi Y., Wang J., Shi Y.;
 "Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic
 amino acid following DegS cleavage.";
 Proc. Natl. Acad. Sci. U.S.A. 106:14837-14842(2009).
 -!- FUNCTION: A site-2 regulated intramembrane protease (S2P) that
     cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the
     transmembrane region of RseA. Part of a regulated intramembrane
     proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release
     the cytoplasmic domain of RseA, residue "Val-148" of RseA may be
     required for this. This provides the cell with sigma-E (RpoE)
     activity through the proteolysis of RseA. Can also cleave
     sequences in transmembrane regions of other proteins (such as
     LacY) as well as liberated signal peptides of beta-lactamase,
     OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within
     the membrane. {ECO:0000269|PubMed:12183368,
     ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:15496982,
     ECO:0000269|PubMed:18268014, ECO:0000269|PubMed:18945679,
     ECO:0000269|PubMed:21810987}.
 -!- COFACTOR:
     Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
 -!- ENZYME REGULATION: Inhibited by Zn(2+) chelator 1,10-
     phenanthroline. {ECO:0000269|PubMed:21810987}.
 -!- SUBUNIT: Interacts with RseA; the third transmembrane domain can
     be cross-linked to the transmembrane domain of RseA.
     {ECO:0000269|PubMed:14633997, ECO:0000269|PubMed:18268014}.
 -!- SUBCELLULAR LOCATION: Cell inner membrane
     {ECO:0000269|PubMed:11689431, ECO:0000269|PubMed:11750129,
     ECO:0000269|PubMed:11867724, ECO:0000269|PubMed:15919996}; Multi-
     pass membrane protein {ECO:0000269|PubMed:11689431,
     ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:11867724,
     ECO:0000269|PubMed:15919996}.
 -!- INDUCTION: Part of the sigma-E regulon. Also has a primary sigma-
     70 factor promoter. {ECO:0000269|PubMed:11274153}.
 -!- DOMAIN: The 2 circularly premutated PDZ domains act to negatively
     regulate protease action on intact RseA; mutations in PDZ-N have a
     more deleterious effect than similar mutations in PDZ-C. A 31
     residue insertion in PDZ-C (between Val-261 and Met-262) domain
     inhibits protease activity, whereas deletion of residues 203-279
     alleviates the PDZ-inhibition, allowing cleavage of intact RseA.
     {ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:14633997,
     ECO:0000269|PubMed:18945679, ECO:0000269|PubMed:19706448,
     ECO:0000269|PubMed:23016873}.
 -!- DISRUPTION PHENOTYPE: Essential. Depletion experiments lead to
     cessation of growth, elongated cells and limited lysis, as well as
     decreased amounts of sigma-E. Not essential in an rseA deletion
     strain, when sigma-E is overexpressed or in ompA-ompC deletion
     strain. In the latter has severely decreased growth at 20 degrees
     Celsius. Accumulation of an RseA proteolysis intermediate.
     {ECO:0000269|PubMed:11274153, ECO:0000269|PubMed:11689431,
     ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:12183368,
     ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:23016873}.
 -!- MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs
     when an extracytoplasmic signal triggers a concerted proteolytic
     cascade to transmit information and elicit cellular responses. A
     membrane-spanning regulatory substrate protein is first cut
     extracytoplasmically (site-1 protease, S1P), then within the
     membrane itself (site-2 protease, S2P, this enzyme), while
     cytoplasmic proteases finish degrading the regulatory protein,
     liberating the effector protein.
 -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
 -!- CAUTION: Was originally thought to be a negative regulator of
     sigma-E function and to act directly on sigma-E and RpoH; this may
     not be physiologically relevant. {ECO:0000305|PubMed:11689431}.
 -----------------------------------------------------------------------
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 EMBL; AF407012; AAL01378.1; -; Genomic_DNA.
 EMBL; U70214; AAB08605.1; -; Genomic_DNA.
 EMBL; U00096; AAC73287.1; -; Genomic_DNA.
 EMBL; AP009048; BAA77851.1; -; Genomic_DNA.
 EMBL; M11330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 PIR; H64741; H64741.
 RefSeq; NP_414718.1; NC_000913.3.
 RefSeq; WP_001295561.1; NZ_LN832404.1.
 PDB; 2ZPL; X-ray; 1.70 A; A/B/C=127-221.
 PDB; 2ZPM; X-ray; 0.98 A; A=222-309.
 PDB; 3ID1; X-ray; 1.67 A; A=127-220.
 PDB; 3ID2; X-ray; 3.09 A; A/B=222-309.
 PDB; 3ID3; X-ray; 2.01 A; A/B=222-309.
 PDB; 3ID4; X-ray; 1.60 A; A=222-307.
 PDBsum; 2ZPL; -.
 PDBsum; 2ZPM; -.
 PDBsum; 3ID1; -.
 PDBsum; 3ID2; -.
 PDBsum; 3ID3; -.
 PDBsum; 3ID4; -.
 ProteinModelPortal; P0AEH1; -.
 SMR; P0AEH1; -.
 BioGrid; 4261736; 75.
 DIP; DIP-48061N; -.
 IntAct; P0AEH1; 1.
 STRING; 316385.ECDH10B_0156; -.
 MEROPS; M50.004; -.
 PaxDb; P0AEH1; -.
 PRIDE; P0AEH1; -.
 EnsemblBacteria; AAC73287; AAC73287; b0176.
 EnsemblBacteria; BAA77851; BAA77851; BAA77851.
 GeneID; 944871; -.
 KEGG; ecj:JW0171; -.
 KEGG; eco:b0176; -.
 PATRIC; fig|1411691.4.peg.2103; -.
 EchoBASE; EB2331; -.
 EcoGene; EG12436; rseP.
 eggNOG; ENOG4105DZP; Bacteria.
 eggNOG; COG0750; LUCA.
 HOGENOM; HOG000006281; -.
 InParanoid; P0AEH1; -.
 KO; K11749; -.
 PhylomeDB; P0AEH1; -.
 BioCyc; EcoCyc:EG12436-MONOMER; -.
 EvolutionaryTrace; P0AEH1; -.
 PRO; PR:P0AEH1; -.
 Proteomes; UP000000318; Chromosome.
 Proteomes; UP000000625; Chromosome.
 GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
 GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
 GO; GO:0043856; F:anti-sigma factor antagonist activity; IMP:EcoCyc.
 GO; GO:0045152; F:antisigma factor binding; IDA:EcoCyc.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0004222; F:metalloendopeptidase activity; IDA:EcoCyc.
 InterPro; IPR001478; PDZ.
 InterPro; IPR004387; Pept_M50_Zn.
 InterPro; IPR008915; Peptidase_M50.
 Pfam; PF00595; PDZ; 1.
 Pfam; PF02163; Peptidase_M50; 1.
 SMART; SM00228; PDZ; 2.
 SUPFAM; SSF50156; SSF50156; 2.
 TIGRFAMs; TIGR00054; TIGR00054; 1.
 PROSITE; PS50106; PDZ; 1.
 PROSITE; PS00142; ZINC_PROTEASE; 1.
 1: Evidence at protein level;
 3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
 Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
 Reference proteome; Repeat; Transmembrane; Transmembrane helix; Zinc.
 CHAIN         1    450       Regulator of sigma-E protease RseP.
                              /FTId=PRO_0000088417.
 TRANSMEM      1     21       Helical. {ECO:0000255}.
 TOPO_DOM     22    103       Periplasmic.
                              {ECO:0000305|PubMed:11750129}.
 TRANSMEM    104    124       Helical. {ECO:0000255}.
 TOPO_DOM    125    375       Cytoplasmic.
                              {ECO:0000305|PubMed:11750129}.
 TRANSMEM    376    396       Helical. {ECO:0000255}.
 TOPO_DOM    397    429       Periplasmic.
                              {ECO:0000305|PubMed:11750129}.
 TRANSMEM    430    450       Helical. {ECO:0000255}.
 DOMAIN      127    220       PDZ 1 (PDZ-N). {ECO:0000255|PROSITE-
                              ProRule:PRU00143}.
 DOMAIN      222    309       PDZ 2 (PDZ-C). {ECO:0000255|PROSITE-
                              ProRule:PRU00143}.
 ACT_SITE     23     23       {ECO:0000305}.
 METAL        22     22       Zinc; catalytic. {ECO:0000305}.
 METAL        26     26       Zinc; catalytic. {ECO:0000255|PROSITE-
                              ProRule:PRU10095}.
 MUTAGEN      22     22       H->A: Loss of protease activity.
                              {ECO:0000269|PubMed:11689431,
                              ECO:0000269|PubMed:11750129,
                              ECO:0000269|PubMed:12183368,
                              ECO:0000269|PubMed:15496982,
                              ECO:0000269|PubMed:18268014,
                              ECO:0000269|PubMed:21810987}.
 MUTAGEN      22     22       H->F: Loss of protease activity of RseA
                              and signal peptides, does not complement
                              deletion mutant. Binds substrate.
                              {ECO:0000269|PubMed:11689431,
                              ECO:0000269|PubMed:11750129,
                              ECO:0000269|PubMed:12183368,
                              ECO:0000269|PubMed:15496982,
                              ECO:0000269|PubMed:18268014,
                              ECO:0000269|PubMed:21810987}.
 MUTAGEN      23     23       E->A: Low basal sigma-E activity, sigma-E
                              not induced. No proteolysis of RseA.
                              {ECO:0000269|PubMed:11750129,
                              ECO:0000269|PubMed:12183369,
                              ECO:0000269|PubMed:18268014}.
 MUTAGEN      23     23       E->D: Behaves like wild-type in vivo,
                              slight reduction in RseA cleavage in
                              vitro. {ECO:0000269|PubMed:11750129,
                              ECO:0000269|PubMed:12183369,
                              ECO:0000269|PubMed:18268014}.
 MUTAGEN      23     23       E->Q: Does not complement deletion
                              mutant. {ECO:0000269|PubMed:11750129,
                              ECO:0000269|PubMed:12183369,
                              ECO:0000269|PubMed:18268014}.
 MUTAGEN      23     23       E->S: Loss of protease activity.
                              {ECO:0000269|PubMed:11750129,
                              ECO:0000269|PubMed:12183369,
                              ECO:0000269|PubMed:18268014}.
 MUTAGEN      26     26       H->F: Does not complement deletion
                              mutant. {ECO:0000269|PubMed:11750129}.
 MUTAGEN     115    115       A->V: No effect. Cleaves RseA without
                              previous DegS cleavage; when associated
                              with R-214.
                              {ECO:0000269|PubMed:18945679}.
 MUTAGEN     145    145       I->N: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:18945679}.
 MUTAGEN     151    151       L->P: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:18945679}.
 MUTAGEN     162    162       W->R: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:18945679}.
 MUTAGEN     169    169       L->S: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:18945679}.
 MUTAGEN     213    213       L->P: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:18945679}.
 MUTAGEN     214    214       G->E,Q: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:14633997,
                              ECO:0000269|PubMed:18945679}.
 MUTAGEN     214    214       G->R: Weakly cuts RseA without previous
                              DegS cleavage. Stronger cleavage; when
                              associated with V-115.
                              {ECO:0000269|PubMed:14633997,
                              ECO:0000269|PubMed:18945679}.
 MUTAGEN     215    215       I->A: No cleavage of RseA in vitro
                              (PubMed:19706448), cleavage of RseA
                              (PubMed:23016873) in vivo.
                              {ECO:0000269|PubMed:19706448,
                              ECO:0000269|PubMed:23016873}.
 MUTAGEN     234    235       AA->KK: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:14633997}.
 MUTAGEN     243    243       G->Q: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:14633997}.
 MUTAGEN     244    244       D->K: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:14633997}.
 MUTAGEN     246    246       I->Y: Cuts RseA without previous DegS
                              cleavage. {ECO:0000269|PubMed:14633997}.
 MUTAGEN     261    261       V->VTDSYTQVASWTEPFPFSIQGDPRSDQETAFV: Does
                              not complement deletion mutant.
                              {ECO:0000269|PubMed:11750129}.
 MUTAGEN     304    304       I->A: No cleavage of RseA in vitro
                              (PubMed:19706448), cleavage of RseA
                              (PubMed:23016873) in vivo.
                              {ECO:0000269|PubMed:19706448,
                              ECO:0000269|PubMed:23016873}.
 MUTAGEN     389    389       N->C,G,L: Decreased substrate binding,
                              retains some proteolytic activity.
                              {ECO:0000269|PubMed:18268014}.
 MUTAGEN     389    389       N->Q: No effect.
                              {ECO:0000269|PubMed:18268014}.
 MUTAGEN     394    394       N->C: Decreased substrate binding,
                              retains some proteolytic activity.
                              {ECO:0000269|PubMed:18268014}.
 MUTAGEN     397    397       P->C: Decreased substrate binding,
                              retains some proteolytic activity.
                              {ECO:0000269|PubMed:18268014}.
 MUTAGEN     399    399       P->C: Decreased substrate binding,
                              retains some proteolytic activity.
                              {ECO:0000269|PubMed:18268014}.
 MUTAGEN     402    402       D->N: Does not complement deletion
                              mutant, loss of protease activity.
                              {ECO:0000269|PubMed:11750129,
                              ECO:0000269|PubMed:12183368}.
 STRAND      130    134       {ECO:0000244|PDB:3ID1}.
 HELIX       139    142       {ECO:0000244|PDB:3ID1}.
 STRAND      150    154       {ECO:0000244|PDB:3ID1}.
 HELIX       162    171       {ECO:0000244|PDB:3ID1}.
 TURN        172    174       {ECO:0000244|PDB:3ID1}.
 STRAND      176    183       {ECO:0000244|PDB:3ID1}.
 STRAND      191    196       {ECO:0000244|PDB:3ID1}.
 TURN        204    206       {ECO:0000244|PDB:3ID1}.
 HELIX       209    212       {ECO:0000244|PDB:3ID1}.
 STRAND      215    217       {ECO:0000244|PDB:3ID1}.
 STRAND      227    229       {ECO:0000244|PDB:2ZPM}.
 STRAND      231    233       {ECO:0000244|PDB:3ID2}.
 HELIX       234    237       {ECO:0000244|PDB:2ZPM}.
 STRAND      245    249       {ECO:0000244|PDB:2ZPM}.
 HELIX       257    266       {ECO:0000244|PDB:2ZPM}.
 STRAND      272    278       {ECO:0000244|PDB:2ZPM}.
 STRAND      281    287       {ECO:0000244|PDB:2ZPM}.
 STRAND      290    292       {ECO:0000244|PDB:2ZPM}.
 STRAND      295    297       {ECO:0000244|PDB:2ZPM}.
 STRAND      299    301       {ECO:0000244|PDB:2ZPM}.
 STRAND      304    307       {ECO:0000244|PDB:3ID4}.
 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

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