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Regulator of sigma-E protease RseP (EC 3.4.24.-) (S2P endopeptidase) (Site-2 protease RseP) (S2P protease RseP) (Site-2-type intramembrane protease)

 RSEP_ECOLI              Reviewed;         450 AA.
P0AEH1; P37764;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
25-OCT-2017, entry version 109.
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 1 (PDZ-
N) have a more deleterious effect than similar mutations in PDZ 2
(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; 2.
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; IPR036034; PDZ_sf.
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. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 222 309 PDZ 2. {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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