SRP54_ECOLI
ID SRP54_ECOLI Reviewed; 453 AA.
AC P0AGD7; P07019; P77007; P77008;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306};
DE Short=Ffh;
DE AltName: Full=p48;
GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306};
GN OrderedLocusNames=b2610, JW5414;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6357787; DOI=10.1002/j.1460-2075.1983.tb01519.x;
RA Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.;
RT "The nucleotide sequence of an Escherichia coli operon containing genes for
RT the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a
RT 21-K polypeptide.";
RL EMBO J. 2:899-905(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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], AND SEQUENCE REVISION.
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 FUNCTION.
RX PubMed=2171778; DOI=10.1016/0092-8674(90)90454-m;
RA Ribes V., Roemisch K., Giner A., Dobberstein B., Tollervey D.;
RT "E. coli 4.5S RNA is part of a ribonucleoprotein particle that has
RT properties related to signal recognition particle.";
RL Cell 63:591-600(1990).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1279430; DOI=10.1038/359741a0;
RA Luirink J., High S., Wood H., Giner A., Tollervey D., Dobberstein B.;
RT "Signal-sequence recognition by an Escherichia coli ribonucleoprotein
RT complex.";
RL Nature 359:741-743(1992).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1331806; DOI=10.1038/359744a0;
RA Phillips G.J., Silhavy T.J.;
RT "The E. coli ffh gene is necessary for viability and efficient protein
RT export.";
RL Nature 359:744-746(1992).
RN [8]
RP FUNCTION, AND SUBUNIT.
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 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 [10]
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 [11]
RP INTERACTION WITH RIBOSOMAL PROTEIN L23 AND NASCENT PROTEIN CHAINS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12756233; DOI=10.1083/jcb.200302130;
RA Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M.,
RA Brunner J., Oudega B., Harms N., Luirink J.;
RT "Interplay of signal recognition particle and trigger factor at L23 near
RT the nascent chain exit site on the Escherichia coli ribosome.";
RL J. Cell Biol. 161:679-684(2003).
RN [12]
RP INTERACTION WITH RIBOSOMAL PROTEIN L23, AND DOMAIN.
RC STRAIN=MRE-600;
RX PubMed=12702815; DOI=10.1261/rna.2196403;
RA Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.;
RT "The signal recognition particle binds to protein L23 at the peptide exit
RT of the Escherichia coli ribosome.";
RL RNA 9:566-573(2003).
RN [13]
RP FUNCTION IN LIPOPROTEIN EXPORT, AND DISRUPTION PHENOTYPE.
RX PubMed=15140892; DOI=10.1074/jbc.m403229200;
RA Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.;
RT "Targeting and translocation of two lipoproteins in Escherichia coli via
RT the SRP/Sec/YidC pathway.";
RL J. Biol. Chem. 279:31026-31032(2004).
RN [14]
RP SIMULTANEOUS BINDING OF TRIGGER FACTOR 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 [15]
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 [16]
RP STRUCTURE BY NMR OF 410-434.
RX PubMed=8898086; DOI=10.1016/0014-5793(96)01019-8;
RA Oh D.-B., Yi G.-S., Chi S.-W., Kim H.;
RT "Structure of a methionine-rich segment of Escherichia coli Ffh protein.";
RL FEBS Lett. 395:160-164(1996).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 371-430 IN COMPLEX WITH 4.5S RNA,
RP AND DOMAIN.
RX PubMed=10678824; DOI=10.1126/science.287.5456.1232;
RA Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A.;
RT "Crystal structure of the ribonucleoprotein core of the signal recognition
RT particle.";
RL Science 287:1232-1239(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 328-432, AND SUBUNIT.
RX PubMed=12269812; DOI=10.1021/bi026163c;
RA Batey R.T., Doudna J.A.;
RT "Structural and energetic analysis of metal ions essential to SRP signal
RT recognition domain assembly.";
RL Biochemistry 41:11703-11710(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (8.00 ANGSTROMS) OF 2-431.
RX PubMed=17086193; DOI=10.1038/nature05326;
RA Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., Sinning I.,
RA Beckmann R.;
RT "Following the signal sequence from ribosomal tunnel exit to signal
RT recognition particle.";
RL Nature 444:507-511(2006).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 329-430.
RX PubMed=17637337; DOI=10.1016/j.str.2007.06.003;
RA Keel A.Y., Rambo R.P., Batey R.T., Kieft J.S.;
RT "A general strategy to solve the phase problem in RNA crystallography.";
RL Structure 15:761-772(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (13.50 ANGSTROMS) OF 371-430.
RX PubMed=21151118; DOI=10.1038/nsmb.1952;
RA Estrozi L.F., Boehringer D., Shan S.O., Ban N., Schaffitzel C.;
RT "Cryo-EM structure of the E. coli translating ribosome in complex with SRP
RT and its receptor.";
RL Nat. Struct. Mol. Biol. 18:88-90(2011).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.94 ANGSTROMS) OF 1-433.
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. Binds to the hydrophobic signal
CC sequence of the ribosome-nascent chain (RNC) as it emerges from the
CC ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic
CC membrane where it interacts with the SRP receptor FtsY. Interaction
CC with FtsY leads to the transfer of the RNC complex to the Sec
CC translocase for insertion into the membrane, the hydrolysis of GTP by
CC both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into
CC the individual components. {ECO:0000255|HAMAP-Rule:MF_00306,
CC ECO:0000269|PubMed:11735405, ECO:0000269|PubMed:11741850,
CC ECO:0000269|PubMed:1279430, ECO:0000269|PubMed:1331806,
CC ECO:0000269|PubMed:15140892, ECO:0000269|PubMed:2171778,
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. Metal ions are essential for
CC the formation and stability of the SRP complex. Interacts with the
CC ribosomes, via ribosomal protein L23. Interacts with FtsY.
CC {ECO:0000255|HAMAP-Rule:MF_00306, ECO:0000269|PubMed:10678824,
CC ECO:0000269|PubMed:12269812, ECO:0000269|PubMed:12702815,
CC ECO:0000269|PubMed:12756233, ECO:0000269|PubMed:1279430,
CC ECO:0000269|PubMed:1331806, ECO:0000269|PubMed:9305630}.
CC -!- INTERACTION:
CC P0AGD7; P10121: ftsY; NbExp=10; IntAct=EBI-369938, EBI-549067;
CC P0AGD7; P0AGB3: rpoH; NbExp=4; IntAct=EBI-369938, EBI-555342;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=The SRP-RNC complex is targeted
CC to the cytoplasmic membrane.
CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which is
CC responsible for interactions with the ribosome, the central G domain,
CC which binds GTP, and the C-terminal M domain, which binds the RNA and
CC the signal sequence of the RNC. {ECO:0000255|HAMAP-Rule:MF_00306,
CC ECO:0000269|PubMed:10678824, ECO:0000269|PubMed:12702815}.
CC -!- DISRUPTION PHENOTYPE: Essential; deletion experiments lead to loss of
CC inner membrane protein targeting. Also leads to reduced targeting of
CC lipoproteins Lpp and BRP. {ECO:0000269|PubMed:11741850,
CC ECO:0000269|PubMed:15140892}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA25957.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X01818; CAA25957.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75659.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16495.2; -; Genomic_DNA.
DR PIR; E65039; E65039.
DR RefSeq; NP_417101.1; NC_000913.3.
DR RefSeq; WP_000460035.1; NZ_STEB01000040.1.
DR PDB; 1DUL; X-ray; 1.80 A; A=371-430.
DR PDB; 1HQ1; X-ray; 1.52 A; A=328-432.
DR PDB; 2J28; EM; 8.00 A; 9=2-431.
DR PDB; 2PXB; X-ray; 2.00 A; A=329-430.
DR PDB; 2PXD; X-ray; 2.00 A; A=329-430.
DR PDB; 2PXE; X-ray; 2.00 A; A=329-430.
DR PDB; 2PXF; X-ray; 2.00 A; A=329-430.
DR PDB; 2PXK; X-ray; 2.00 A; A=329-430.
DR PDB; 2PXL; X-ray; 2.50 A; A=329-430.
DR PDB; 2PXP; X-ray; 2.50 A; A=329-430.
DR PDB; 2PXQ; X-ray; 2.50 A; A=329-430.
DR PDB; 2PXT; X-ray; 2.50 A; A=329-430.
DR PDB; 2PXU; X-ray; 2.50 A; A=329-430.
DR PDB; 2PXV; X-ray; 2.00 A; A=329-430.
DR PDB; 2XKV; EM; 13.50 A; C=371-430.
DR PDB; 2XXA; X-ray; 3.94 A; A/C=1-433.
DR PDB; 3LQX; X-ray; 1.93 A; A=329-428.
DR PDB; 4C7O; X-ray; 2.60 A; A/C=1-298.
DR PDB; 5AKA; EM; 5.70 A; 5=328-436.
DR PDB; 5GAD; EM; 3.70 A; i=4-434.
DR PDB; 5GAF; EM; 4.30 A; i=1-434.
DR PDB; 5GAG; EM; 3.80 A; i=4-434.
DR PDB; 5GAH; EM; 3.80 A; i=1-434.
DR PDB; 5NCO; EM; 4.80 A; i=4-434.
DR PDB; 7O9I; X-ray; 2.49 A; A=3-299.
DR PDBsum; 1DUL; -.
DR PDBsum; 1HQ1; -.
DR PDBsum; 2J28; -.
DR PDBsum; 2PXB; -.
DR PDBsum; 2PXD; -.
DR PDBsum; 2PXE; -.
DR PDBsum; 2PXF; -.
DR PDBsum; 2PXK; -.
DR PDBsum; 2PXL; -.
DR PDBsum; 2PXP; -.
DR PDBsum; 2PXQ; -.
DR PDBsum; 2PXT; -.
DR PDBsum; 2PXU; -.
DR PDBsum; 2PXV; -.
DR PDBsum; 2XKV; -.
DR PDBsum; 2XXA; -.
DR PDBsum; 3LQX; -.
DR PDBsum; 4C7O; -.
DR PDBsum; 5AKA; -.
DR PDBsum; 5GAD; -.
DR PDBsum; 5GAF; -.
DR PDBsum; 5GAG; -.
DR PDBsum; 5GAH; -.
DR PDBsum; 5NCO; -.
DR PDBsum; 7O9I; -.
DR AlphaFoldDB; P0AGD7; -.
DR SMR; P0AGD7; -.
DR BioGRID; 4262086; 316.
DR BioGRID; 851437; 1.
DR DIP; DIP-31865N; -.
DR IntAct; P0AGD7; 23.
DR STRING; 511145.b2610; -.
DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family.
DR MetOSite; P0AGD7; -.
DR jPOST; P0AGD7; -.
DR PaxDb; P0AGD7; -.
DR PRIDE; P0AGD7; -.
DR EnsemblBacteria; AAC75659; AAC75659; b2610.
DR EnsemblBacteria; BAA16495; BAA16495; BAA16495.
DR GeneID; 67414072; -.
DR GeneID; 947102; -.
DR KEGG; ecj:JW5414; -.
DR KEGG; eco:b2610; -.
DR PATRIC; fig|1411691.4.peg.4129; -.
DR EchoBASE; EB0296; -.
DR eggNOG; COG0541; Bacteria.
DR HOGENOM; CLU_009301_6_0_6; -.
DR InParanoid; P0AGD7; -.
DR OMA; DTAGRHK; -.
DR PhylomeDB; P0AGD7; -.
DR BioCyc; EcoCyc:EG10300-MON; -.
DR BRENDA; 3.6.5.4; 2026.
DR EvolutionaryTrace; P0AGD7; -.
DR PRO; PR:P0AGD7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:EcoliWiki.
DR GO; GO:0048500; C:signal recognition particle; IMP:EcoliWiki.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IDA:EcoliWiki.
DR GO; GO:0003924; F:GTPase activity; IMP:EcoCyc.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:EcoliWiki.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00306; SRP54; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR InterPro; IPR004780; SRP.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR11564; PTHR11564; 1.
DR PANTHER; PTHR11564:SF7; PTHR11564:SF7; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF02978; SRP_SPB; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00959; ffh; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..453
FT /note="Signal recognition particle protein"
FT /id="PRO_0000101153"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 24..40
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:4C7O"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:4C7O"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:1HQ1"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:1HQ1"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:1HQ1"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:1HQ1"
FT HELIX 396..405
FT /evidence="ECO:0007829|PDB:1HQ1"
FT HELIX 410..430
FT /evidence="ECO:0007829|PDB:1HQ1"
SQ SEQUENCE 453 AA; 49787 MW; E9C7A7101CC04D66 CRC64;
MFDNLTDRLS RTLRNISGRG RLTEDNVKDT LREVRMALLE ADVALPVVRE FINRVKEKAV
GHEVNKSLTP GQEFVKIVRN ELVAAMGEEN QTLNLAAQPP AVVLMAGLQG AGKTTSVGKL
GKFLREKHKK KVLVVSADVY RPAAIKQLET LAEQVGVDFF PSDVGQKPVD IVNAALKEAK
LKFYDVLLVD TAGRLHVDEA MMDEIKQVHA SINPVETLFV VDAMTGQDAA NTAKAFNEAL
PLTGVVLTKV DGDARGGAAL SIRHITGKPI KFLGVGEKTE ALEPFHPDRI ASRILGMGDV
LSLIEDIESK VDRAQAEKLA SKLKKGDGFD LNDFLEQLRQ MKNMGGMASL MGKLPGMGQI
PDNVKSQMDD KVLVRMEAII NSMTMKERAK PEIIKGSRKR RIAAGCGMQV QDVNRLLKQF
DDMQRMMKKM KKGGMAKMMR SMKGMMPPGF PGR
