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 25-MAY-2022, entry version 148. 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}; 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; 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 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 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-MONOMER; -. 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 NP_BIND 107..114 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306" FT NP_BIND 190..194 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306" FT NP_BIND 248..251 FT /note="GTP" 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 //