FTSY_ECOLI
ID FTSY_ECOLI Reviewed; 497 AA.
AC P10121; Q2M7C7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920};
DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920};
GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920};
GN OrderedLocusNames=b3464, JW3429;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3025556; DOI=10.1007/bf02428043;
RA Gill D.R., Hatfull G.F., Salmond G.P.C.;
RT "A new cell division operon in Escherichia coli.";
RL Mol. Gen. Genet. 205:134-145(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-11 AND 15-25, SUBCELLULAR LOCATION, DOMAIN, CLEAVAGE,
RP AND MUTAGENESIS OF GLY-14.
RX PubMed=18281057; DOI=10.1016/j.jmb.2008.01.040;
RA Weiche B., Burk J., Angelini S., Schiltz E., Thumfart J.O., Koch H.G.;
RT "A cleavable N-terminal membrane anchor is involved in membrane binding of
RT the Escherichia coli SRP receptor.";
RL J. Mol. Biol. 377:761-773(2008).
RN [6]
RP CHARACTERIZATION.
RX PubMed=2161989; DOI=10.1111/j.1365-2958.1990.tb00626.x;
RA Gill D.R., Salmond G.P.C.;
RT "The identification of the Escherichia coli ftsY gene product: an unusual
RT protein.";
RL Mol. Microbiol. 4:575-583(1990).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=8194520; DOI=10.1002/j.1460-2075.1994.tb06511.x;
RA Luirink J., ten Hagen-Jongman C.M., van der Weijden C.C., Oudega B.,
RA High S., Dobberstein B., Kusters R.;
RT "An alternative protein targeting pathway in Escherichia coli: studies on
RT the role of FtsY.";
RL EMBO J. 13:2289-2296(1994).
RN [8]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=9305630; DOI=10.1093/emboj/16.16.4880;
RA Powers T., Walter P.;
RT "Co-translational protein targeting catalyzed by the Escherichia coli
RT signal recognition particle and its receptor.";
RL EMBO J. 16:4880-4886(1997).
RN [9]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=9177162; DOI=10.1073/pnas.94.12.6025;
RA Zelazny A., Seluanov A., Cooper A., Bibi E.;
RT "The NG domain of the prokaryotic signal recognition particle receptor,
RT FtsY, is fully functional when fused to an unrelated integral membrane
RT polypeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6025-6029(1997).
RN [10]
RP FUNCTION, GTPASE ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=11735405; DOI=10.1021/bi011639y;
RA Peluso P., Shan S.O., Nock S., Herschlag D., Walter P.;
RT "Role of SRP RNA in the GTPase cycles of Ffh and FtsY.";
RL Biochemistry 40:15224-15233(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=11353766; DOI=10.1074/jbc.m011331200;
RA Millman J.S., Qi H.Y., Vulcu F., Bernstein H.D., Andrews D.W.;
RT "FtsY binds to the Escherichia coli inner membrane via interactions with
RT phosphatidylethanolamine and membrane proteins.";
RL J. Biol. Chem. 276:25982-25989(2001).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=11741850; DOI=10.1128/jb.184.1.111-118.2002;
RA Tian H., Beckwith J.;
RT "Genetic screen yields mutations in genes encoding all known components of
RT the Escherichia coli signal recognition particle pathway.";
RL J. Bacteriol. 184:111-118(2002).
RN [13]
RP FUNCTION, AND BINDING OF FTSY AND SRP TO THE RIBOSOME.
RC STRAIN=MRE-600;
RX PubMed=15148364; DOI=10.1073/pnas.0402231101;
RA Buskiewicz I., Deuerling E., Gu S.-Q., Joeckel J., Rodnina M.V., Bukau B.,
RA Wintermeyer W.;
RT "Trigger factor binds to ribosome-signal-recognition particle (SRP)
RT complexes and is excluded by binding of the SRP receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7902-7906(2004).
RN [14]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=17726013; DOI=10.1074/jbc.m705429200;
RA Bahari L., Parlitz R., Eitan A., Stjepanovic G., Bochkareva E.S.,
RA Sinning I., Bibi E.;
RT "Membrane targeting of ribosomes and their release require distinct and
RT separable functions of FtsY.";
RL J. Biol. Chem. 282:32168-32175(2007).
RN [15]
RP FUNCTION, AND GTPASE ACTIVITY.
RX PubMed=17682051; DOI=10.1083/jcb.200702018;
RA Shan S.O., Chandrasekar S., Walter P.;
RT "Conformational changes in the GTPase modules of the signal reception
RT particle and its receptor drive initiation of protein translocation.";
RL J. Cell Biol. 178:611-620(2007).
RN [16]
RP DOMAIN, LIPID-BINDING SITES, AND SUBCELLULAR LOCATION.
RX PubMed=19414018; DOI=10.1016/j.jmb.2009.04.061;
RA Braig D., Bar C., Thumfart J.O., Koch H.G.;
RT "Two cooperating helices constitute the lipid-binding domain of the
RT bacterial SRP receptor.";
RL J. Mol. Biol. 390:401-413(2009).
RN [17]
RP INTERACTION WITH SECY.
RX PubMed=21255212; DOI=10.1111/j.1600-0854.2011.01167.x;
RA Kuhn P., Weiche B., Sturm L., Sommer E., Drepper F., Warscheid B.,
RA Sourjik V., Koch H.G.;
RT "The bacterial SRP receptor, SecA and the ribosome use overlapping binding
RT sites on the SecY translocon.";
RL Traffic 12:563-578(2011).
RN [18]
RP REVIEW.
RX PubMed=20682283; DOI=10.1016/j.bbamem.2010.07.025;
RA Bibi E.;
RT "Early targeting events during membrane protein biogenesis in Escherichia
RT coli.";
RL Biochim. Biophys. Acta 1808:841-850(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 201-495, AND DOMAIN.
RX PubMed=9002525; DOI=10.1038/385365a0;
RA Montoya G., Svensson C., Luirink J., Sinning I.;
RT "Crystal structure of the NG domain from the signal-recognition particle
RT receptor FtsY.";
RL Nature 385:365-368(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 196-497, AND DOMAIN.
RX PubMed=17726012; DOI=10.1074/jbc.m705430200;
RA Parlitz R., Eitan A., Stjepanovic G., Bahari L., Bange G., Bibi E.,
RA Sinning I.;
RT "Escherichia coli signal recognition particle receptor FtsY contains an
RT essential and autonomous membrane-binding amphipathic helix.";
RL J. Biol. Chem. 282:32176-32184(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBCELLULAR LOCATION.
RX PubMed=21543314; DOI=10.1074/jbc.m110.212340;
RA Stjepanovic G., Kapp K., Bange G., Graf C., Parlitz R., Wild K.,
RA Mayer M.P., Sinning I.;
RT "Lipids trigger a conformational switch that regulates signal recognition
RT particle (SRP)-mediated protein targeting.";
RL J. Biol. Chem. 286:23489-23497(2011).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.94 ANGSTROMS) OF 196-497 IN COMPLEX WITH SRP.
RX PubMed=21330537; DOI=10.1126/science.1196473;
RA Ataide S.F., Schmitz N., Shen K., Ke A., Shan S.O., Doudna J.A., Ban N.;
RT "The crystal structure of the signal recognition particle in complex with
RT its receptor.";
RL Science 331:881-886(2011).
CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC proteins into the cytoplasmic membrane. Acts as a receptor for the
CC complex formed by the signal recognition particle (SRP) and the
CC ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the
CC transfer of the RNC complex to the Sec translocase for insertion into
CC the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the
CC dissociation of the SRP-FtsY complex into the individual components.
CC {ECO:0000255|HAMAP-Rule:MF_00920, ECO:0000269|PubMed:11735405,
CC ECO:0000269|PubMed:11741850, ECO:0000269|PubMed:15148364,
CC ECO:0000269|PubMed:17682051, ECO:0000269|PubMed:8194520,
CC ECO:0000269|PubMed:9305630}.
CC -!- ACTIVITY REGULATION: Conformation of the Ffh-FtsY complex and
CC regulation of its GTPase activity are modulated by the 4.5S RNA.
CC Formation of the FfH-FtsY complex leads to a mutual stimulation of both
CC GTPases. {ECO:0000269|PubMed:11735405}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein
CC composed of Ffh and a 4.5S RNA molecule. Binds to SecY.
CC {ECO:0000255|HAMAP-Rule:MF_00920, ECO:0000269|PubMed:21330537,
CC ECO:0000269|PubMed:9305630}.
CC -!- INTERACTION:
CC P10121; P0AGD7: ffh; NbExp=10; IntAct=EBI-549067, EBI-369938;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11353766,
CC ECO:0000269|PubMed:17726013, ECO:0000269|PubMed:18281057,
CC ECO:0000269|PubMed:19414018, ECO:0000269|PubMed:21543314,
CC ECO:0000269|PubMed:8194520, ECO:0000269|PubMed:9177162}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11353766,
CC ECO:0000269|PubMed:17726013, ECO:0000269|PubMed:18281057,
CC ECO:0000269|PubMed:19414018, ECO:0000269|PubMed:21543314,
CC ECO:0000269|PubMed:8194520, ECO:0000269|PubMed:9177162}; Cytoplasmic
CC side {ECO:0000269|PubMed:11353766, ECO:0000269|PubMed:17726013,
CC ECO:0000269|PubMed:18281057, ECO:0000269|PubMed:19414018,
CC ECO:0000269|PubMed:21543314, ECO:0000269|PubMed:8194520,
CC ECO:0000269|PubMed:9177162}. Cytoplasm {ECO:0000269|PubMed:18281057,
CC ECO:0000269|PubMed:8194520}. Note=Distributed between the membrane and
CC the cytoplasm (PubMed:18281057, PubMed:8194520). Binding to the
CC membrane probably occurs initially through phospholipid binding, which
CC allows a strong membrane contact, followed by interaction with a
CC membrane protein (PubMed:11353766). Targeting of FtsY to the membrane
CC is essential for proper function (PubMed:9177162). The stability of
CC this membrane contact may be regulated by cleavage of helix 1
CC (PubMed:19414018). {ECO:0000269|PubMed:11353766,
CC ECO:0000269|PubMed:18281057, ECO:0000269|PubMed:19414018,
CC ECO:0000269|PubMed:8194520, ECO:0000269|PubMed:9177162}.
CC -!- DOMAIN: Contains an acidic N-terminal A domain, a central N domain and
CC a C-terminal GTPase G domain that can bind and hydrolyze GTP. Contains
CC at least two lipid-binding sites. The first site contains the first 14
CC amino acids (helix 1) and the second binding site is an amphipathic
CC alpha-helix located at the interface between the A- and the N-domain
CC (helix 2). {ECO:0000255|HAMAP-Rule:MF_00920,
CC ECO:0000269|PubMed:17726012, ECO:0000269|PubMed:17726013,
CC ECO:0000269|PubMed:18281057, ECO:0000269|PubMed:19414018,
CC ECO:0000269|PubMed:9002525, ECO:0000269|PubMed:9177162,
CC ECO:0000269|PubMed:9305630}.
CC -!- PTM: Proteolytically cleaved. The cleavage may regulate function and
CC subcellular location of FtsY. Full-length FtsY is found primarily
CC associated with the membrane, while cleaved protein is predominantly
CC present in the cytoplasm. {ECO:0000269|PubMed:18281057}.
CC -!- DISRUPTION PHENOTYPE: Deletion affects both cell morphology and protein
CC export. Mutants are defective in the insertion into the cytoplasmic
CC membrane of three topologically distinct membrane proteins, MalF, AcrB
CC and FtsQ. {ECO:0000269|PubMed:11741850, ECO:0000269|PubMed:8194520}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR EMBL; X04398; CAA27984.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18439.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76489.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77829.1; -; Genomic_DNA.
DR PIR; S03130; CEECFY.
DR RefSeq; NP_417921.1; NC_000913.3.
DR RefSeq; WP_001040654.1; NZ_SSZK01000008.1.
DR PDB; 1FTS; X-ray; 2.20 A; A=201-495.
DR PDB; 2QY9; X-ray; 1.90 A; A=196-497.
DR PDB; 2XXA; X-ray; 3.94 A; B/D=196-497.
DR PDB; 2YHS; X-ray; 1.60 A; A=1-497.
DR PDB; 3ZN8; EM; 12.00 A; D=201-495.
DR PDB; 4C7O; X-ray; 2.60 A; B/D=224-497.
DR PDB; 5GAD; EM; 3.70 A; l=1-497.
DR PDB; 5NCO; EM; 4.80 A; l=224-494.
DR PDB; 5NIY; X-ray; 1.70 A; A=195-497.
DR PDB; 6CQP; X-ray; 1.45 A; A/B=196-497.
DR PDB; 6CS8; X-ray; 1.75 A; A/B=196-497.
DR PDB; 6CVD; X-ray; 1.78 A; A/B=196-497.
DR PDB; 6DLX; X-ray; 1.85 A; A/B=196-497.
DR PDB; 6FPK; X-ray; 1.95 A; A=221-280.
DR PDB; 6FPR; X-ray; 2.65 A; A/B=221-280.
DR PDB; 6FQD; X-ray; 2.10 A; A/B=221-497.
DR PDB; 6N5I; X-ray; 1.50 A; A/B=196-497.
DR PDB; 6N5J; X-ray; 1.37 A; A/B=196-497.
DR PDB; 6N6N; X-ray; 1.88 A; A/B=196-497.
DR PDB; 6N9B; X-ray; 1.22 A; A/B=196-497.
DR PDB; 6NC1; X-ray; 1.60 A; A/B=196-497.
DR PDB; 6NC4; X-ray; 1.60 A; A/B=196-497.
DR PDBsum; 1FTS; -.
DR PDBsum; 2QY9; -.
DR PDBsum; 2XXA; -.
DR PDBsum; 2YHS; -.
DR PDBsum; 3ZN8; -.
DR PDBsum; 4C7O; -.
DR PDBsum; 5GAD; -.
DR PDBsum; 5NCO; -.
DR PDBsum; 5NIY; -.
DR PDBsum; 6CQP; -.
DR PDBsum; 6CS8; -.
DR PDBsum; 6CVD; -.
DR PDBsum; 6DLX; -.
DR PDBsum; 6FPK; -.
DR PDBsum; 6FPR; -.
DR PDBsum; 6FQD; -.
DR PDBsum; 6N5I; -.
DR PDBsum; 6N5J; -.
DR PDBsum; 6N6N; -.
DR PDBsum; 6N9B; -.
DR PDBsum; 6NC1; -.
DR PDBsum; 6NC4; -.
DR AlphaFoldDB; P10121; -.
DR SMR; P10121; -.
DR BioGRID; 4262499; 595.
DR BioGRID; 852287; 1.
DR DIP; DIP-9709N; -.
DR IntAct; P10121; 8.
DR STRING; 511145.b3464; -.
DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family.
DR jPOST; P10121; -.
DR PaxDb; P10121; -.
DR PRIDE; P10121; -.
DR EnsemblBacteria; AAC76489; AAC76489; b3464.
DR EnsemblBacteria; BAE77829; BAE77829; BAE77829.
DR GeneID; 947978; -.
DR KEGG; ecj:JW3429; -.
DR KEGG; eco:b3464; -.
DR PATRIC; fig|1411691.4.peg.3261; -.
DR EchoBASE; EB0342; -.
DR eggNOG; COG0552; Bacteria.
DR HOGENOM; CLU_009301_0_0_6; -.
DR InParanoid; P10121; -.
DR OMA; GIEATDY; -.
DR PhylomeDB; P10121; -.
DR BioCyc; EcoCyc:EG10346-MON; -.
DR BRENDA; 3.6.5.4; 2026.
DR EvolutionaryTrace; P10121; -.
DR PRO; PR:P10121; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IDA:EcoCyc.
DR DisProt; DP00896; -.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00920; FtsY; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004390; SR_rcpt_FtsY.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR43134:SF7; PTHR43134:SF7; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00064; ftsY; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18281057"
FT CHAIN 2..497
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000101131"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 300..307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 382..386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 446..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT SITE 14..15
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:18281057"
FT MUTAGEN 14
FT /note="G->A: Blocks proteolytic cleavage and impairs
FT activity in cotranslational targeting."
FT /evidence="ECO:0000269|PubMed:18281057"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 242..258
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2QY9"
FT HELIX 390..404
FT /evidence="ECO:0007829|PDB:6N9B"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 425..437
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:2YHS"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:6N9B"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:6N9B"
FT HELIX 485..493
FT /evidence="ECO:0007829|PDB:6N9B"
SQ SEQUENCE 497 AA; 54513 MW; EBE640072B5D1021 CRC64;
MAKEKKRGFF SWLGFGQKEQ TPEKETEVQN EQPVVEEIVQ AQEPVKASEQ AVEEQPQAHT
EAEAETFAAD VVEVTEQVAE SEKAQPEAEV VAQPEPVVEE TPEPVAIERE ELPLPEDVNA
EAVSPEEWQA EAETVEIVEA AEEEAAKEEI TDEELETALA AEAAEEAVMV VPPAEEEQPV
EEIAQEQEKP TKEGFFARLK RSLLKTKENL GSGFISLFRG KKIDDDLFEE LEEQLLIADV
GVETTRKIIT NLTEGASRKQ LRDAEALYGL LKEEMGEILA KVDEPLNVEG KAPFVILMVG
VNGVGKTTTI GKLARQFEQQ GKSVMLAAGD TFRAAAVEQL QVWGQRNNIP VIAQHTGADS
ASVIFDAIQA AKARNIDVLI ADTAGRLQNK SHLMEELKKI VRVMKKLDVE APHEVMLTID
ASTGQNAVSQ AKLFHEAVGL TGITLTKLDG TAKGGVIFSV ADQFGIPIRY IGVGERIEDL
RPFKADDFIE ALFARED
