SECY_ECOLI
ID SECY_ECOLI Reviewed; 443 AA.
AC P0AGA2; P03844; Q2M6W5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY; Synonyms=prlA; OrderedLocusNames=b3300, JW3262;
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=6222285; DOI=10.1093/nar/11.9.2599;
RA Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.;
RT "The spc ribosomal protein operon of Escherichia coli: sequence and
RT cotranscription of the ribosomal protein genes and a protein export gene.";
RL Nucleic Acids Res. 11:2599-2616(1983).
RN [2]
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 [3]
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 [4]
RP TOPOLOGY.
RX PubMed=2828030; DOI=10.1002/j.1460-2075.1987.tb02670.x;
RA Akiyama Y., Ito K.;
RT "Topology analysis of the SecY protein, an integral membrane protein
RT involved in protein export in Escherichia coli.";
RL EMBO J. 6:3465-3470(1987).
RN [5]
RP MUTANT SECY100.
RX PubMed=2646297; DOI=10.1128/jb.171.3.1742-1743.1989;
RA Ito K., Hirota Y., Akiyama Y.;
RT "Temperature-sensitive sec mutants of Escherichia coli: inhibition of
RT protein export at the permissive temperature.";
RL J. Bacteriol. 171:1742-1743(1989).
RN [6]
RP REQUIRED FOR ITS OWN INSERTION INTO MEMBRANES.
RC STRAIN=K12 / MC4100;
RX PubMed=2535843; DOI=10.1016/s0021-9258(17)31277-2;
RA Akiyama Y., Ito K.;
RT "Export of Escherichia coli alkaline phosphatase attached to an integral
RT membrane protein, SecY.";
RL J. Biol. Chem. 264:437-442(1989).
RN [7]
RP MUTANTS SECY39 AND SECY40.
RX PubMed=2254269; DOI=10.1128/jb.172.12.7005-7010.1990;
RA Baba T., Jacq A., Brickman E., Beckwith J., Taura T., Ueguchi C.,
RA Akiyama Y., Ito K.;
RT "Characterization of cold-sensitive secY mutants of Escherichia coli.";
RL J. Bacteriol. 172:7005-7010(1990).
RN [8]
RP MUTANTS SECY121 AND SECY161.
RX PubMed=2007553; DOI=10.1128/jb.173.7.2289-2296.1991;
RA Sako T.;
RT "Novel prlA alleles defective in supporting staphylokinase processing in
RT Escherichia coli.";
RL J. Bacteriol. 173:2289-2296(1991).
RN [9]
RP CHARACTERIZATION.
RX PubMed=1633829; DOI=10.1111/j.1432-1033.1992.tb17111.x;
RA Swidersky U.E., Rienhoefer-Schweer A., Werner P.K., Ernst F., Benson S.A.,
RA Hoffschulte H.K., Mueller M.;
RT "Biochemical analysis of the biogenesis and function of the Escherichia
RT coli export factor SecY.";
RL Eur. J. Biochem. 207:803-811(1992).
RN [10]
RP MUTANTS.
RX PubMed=8253067; DOI=10.1002/j.1460-2075.1993.tb06013.x;
RA Osborne R.S., Silhavy T.J.;
RT "PrlA suppressor mutations cluster in regions corresponding to three
RT distinct topological domains.";
RL EMBO J. 12:3391-3398(1993).
RN [11]
RP MUTAGENESIS OF GLY-240.
RC STRAIN=K12 / MC4100;
RX PubMed=8183945; DOI=10.1073/pnas.91.10.4539;
RA Baba T., Taura T., Shimoike T., Akiyama Y., Yoshihisa T., Ito K.;
RT "A cytoplasmic domain is important for the formation of a SecY-SecE
RT translocator complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4539-4543(1994).
RN [12]
RP MUTANTS.
RX PubMed=7889938; DOI=10.1002/j.1460-2075.1995.tb07070.x;
RA Flower A.M., Osborne R.S., Silhavy T.J.;
RT "The allele-specific synthetic lethality of prlA-prlG double mutants
RT predicts interactive domains of SecY and SecE.";
RL EMBO J. 14:884-893(1995).
RN [13]
RP DEGRADATION BY FTSH.
RX PubMed=7753838; DOI=10.1073/pnas.92.10.4532;
RA Kihara A., Akiyama Y., Ito K.;
RT "FtsH is required for proteolytic elimination of uncomplexed forms of SecY,
RT an essential protein translocase subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4532-4536(1995).
RN [14]
RP INTERACTION WITH FTSQ BEFORE YIDC.
RX PubMed=11415986; DOI=10.1093/embo-reports/kve108;
RA Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W.,
RA Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.;
RT "Sec-dependent membrane protein insertion: sequential interaction of
RT nascent FtsQ with SecY and YidC.";
RL EMBO Rep. 2:524-529(2001).
RN [15]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [16]
RP INTERACTION WITH SECA, AND CHARACTERIZATION OF THE TRANSLOCATING PORE.
RX PubMed=17418789; DOI=10.1016/j.cell.2007.02.036;
RA Osborne A.R., Rapoport T.A.;
RT "Protein translocation is mediated by oligomers of the SecY complex with
RT one SecY copy forming the channel.";
RL Cell 129:97-110(2007).
RN [17]
RP COMPLEX DEGRADATION.
RC STRAIN=K12 / MC4100;
RX PubMed=19661432; DOI=10.1126/science.1172221;
RA van Stelten J., Silva F., Belin D., Silhavy T.J.;
RT "Effects of antibiotics and a proto-oncogene homolog on destruction of
RT protein translocator SecY.";
RL Science 325:753-756(2009).
RN [18]
RP CHARACTERIZATION OF CHANNEL OPENING, AND MUTAGENESIS OF 60-ILE--ARG-74;
RP 65-ASN--GLY-70; PHE-67 AND ILE-408.
RX PubMed=17531809; DOI=10.1016/j.molcel.2007.03.022;
RA Saparov S.M., Erlandson K., Cannon K., Schaletzky J., Schulman S.,
RA Rapoport T.A., Pohl P.;
RT "Determining the conductance of the SecY protein translocation channel for
RT small molecules.";
RL Mol. Cell 26:501-509(2007).
RN [19]
RP MUTAGENESIS OF 60-ILE--ARG-74 AND 65-ASN--GLY-70.
RX PubMed=17531810; DOI=10.1016/j.molcel.2007.05.002;
RA Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.;
RT "The plug domain of the SecY protein stabilizes the closed state of the
RT translocation channel and maintains a membrane seal.";
RL Mol. Cell 26:511-521(2007).
RN [20]
RP MUTAGENESIS OF 424-MET--ARG-443.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=20855604; DOI=10.1073/pnas.1012556107;
RA Egea P.F., Stroud R.M.;
RT "Lateral opening of a translocon upon entry of protein suggests the
RT mechanism of insertion into membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17182-17187(2010).
RN [21]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=27435098; DOI=10.1042/bcj20160545;
RA Komar J., Alvira S., Schulze R.J., Martin R., Lycklama a Nijeholt J.A.,
RA Lee S.C., Dafforn T.R., Deckers-Hebestreit G., Berger I., Schaffitzel C.,
RA Collinson I.;
RT "Membrane protein insertion and assembly by the bacterial holo-translocon
RT SecYEG-SecDF-YajC-YidC.";
RL Biochem. J. 473:3341-3354(2016).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 1-436 IN COMPLEX WITH
RP THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
RC STRAIN=MRE-600;
RX PubMed=16292303; DOI=10.1038/nature04133;
RA Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III,
RA Ban N., Frank J.;
RT "Structure of the E. coli protein-conducting channel bound to a translating
RT ribosome.";
RL Nature 438:318-324(2005).
RN [23]
RP STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A
RP NASCENT POLYPEPTIDE CHAIN.
RX PubMed=21499241; DOI=10.1038/nsmb.2026;
RA Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B.,
RA Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R.;
RT "Cryo-EM structure of the ribosome-SecYE complex in the membrane
RT environment.";
RL Nat. Struct. Mol. Biol. 18:614-621(2011).
RN [24]
RP REVIEW.
RX PubMed=2202723; DOI=10.1007/bf00763172;
RA Ito K.;
RT "Structure, function, and biogenesis of SecY, an integral membrane protein
RT involved in protein export.";
RL J. Bioenerg. Biomembr. 22:353-367(1990).
RN [25]
RP REVIEW.
RX PubMed=18078384; DOI=10.1146/annurev.biochem.77.061606.160747;
RA Driessen A.J., Nouwen N.;
RT "Protein translocation across the bacterial cytoplasmic membrane.";
RL Annu. Rev. Biochem. 77:643-667(2008).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently. SecY
CC is required to insert newly synthesized SecY into the inner membrane.
CC Overexpression of some hybrid proteins has been thought to jam the
CC protein secretion apparatus resulting in cell death; while this may be
CC true, overexpression also results in FtsH-mediated degradation of SecY.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. Interacts with the ribosome. Interacts with SecDF-YajC and
CC YidC; YidC interacts with nascent inner membrane proteins after SecY.
CC The SecDF-YidC-YajC translocase forms a supercomplex with SecYEG,
CC called the holo-translocon (HTL) (PubMed:27435098). The stoichiometry
CC of the super complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the
CC reconstituted complex (with SecDF) but as no antibody is available it
CC could not be quantified (PubMed:27435098). SecY probably contacts the
CC 23S rRNA and possibly also ribosomal protein L23 during ribosome
CC docking. A single SecY molecule forms the translocating pore, although
CC interaction with SecA may require oligomers.
CC {ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:17418789,
CC ECO:0000269|PubMed:27435098}.
CC -!- INTERACTION:
CC P0AGA2; P0A910: ompA; NbExp=2; IntAct=EBI-761422, EBI-371347;
CC P0AGA2; P10408: secA; NbExp=6; IntAct=EBI-761422, EBI-543213;
CC P0AGA2; P0AG96: secE; NbExp=5; IntAct=EBI-761422, EBI-6404267;
CC P0AGA2; P0AG99: secG; NbExp=3; IntAct=EBI-761422, EBI-6404248;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- PTM: SecY that is not part of the protein translocation apparatus is
CC degraded by FtsH. Also degraded by FtsH when the SecYEG complex is
CC jammed, or upon treatment with antibiotics that block translation
CC elongation such as chloramphenicol.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; X01563; CAA25725.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58097.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76325.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77991.1; -; Genomic_DNA.
DR PIR; A04473; QQECSY.
DR RefSeq; NP_417759.1; NC_000913.3.
DR RefSeq; WP_001118861.1; NZ_STEB01000038.1.
DR PDB; 2AKH; EM; 14.90 A; B/Y=1-436.
DR PDB; 2AKI; EM; 14.90 A; B/Y=1-436.
DR PDB; 3J45; EM; 9.50 A; y=6-440.
DR PDB; 3J46; EM; 10.10 A; y=6-440.
DR PDB; 4V6M; EM; -; A=8-442.
DR PDB; 5ABB; EM; 8.00 A; A=1-443.
DR PDB; 5GAE; EM; 3.33 A; g=1-443.
DR PDB; 5MG3; EM; 14.00 A; Y=1-443.
DR PDB; 5NCO; EM; 4.80 A; g=14-429.
DR PDB; 6R7L; EM; 6.00 A; Y=1-443.
DR PDBsum; 2AKH; -.
DR PDBsum; 2AKI; -.
DR PDBsum; 3J45; -.
DR PDBsum; 3J46; -.
DR PDBsum; 4V6M; -.
DR PDBsum; 5ABB; -.
DR PDBsum; 5GAE; -.
DR PDBsum; 5MG3; -.
DR PDBsum; 5NCO; -.
DR PDBsum; 6R7L; -.
DR AlphaFoldDB; P0AGA2; -.
DR SMR; P0AGA2; -.
DR BioGRID; 4263404; 365.
DR ComplexPortal; CPX-1095; Holo-translocon SecYEG-SecDF-YajC-YidC complex.
DR ComplexPortal; CPX-1096; Protein-conducting channel SecYEG complex.
DR DIP; DIP-59302N; -.
DR IntAct; P0AGA2; 5.
DR STRING; 511145.b3300; -.
DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family.
DR jPOST; P0AGA2; -.
DR PaxDb; P0AGA2; -.
DR PRIDE; P0AGA2; -.
DR EnsemblBacteria; AAC76325; AAC76325; b3300.
DR EnsemblBacteria; BAE77991; BAE77991; BAE77991.
DR GeneID; 67415341; -.
DR GeneID; 947799; -.
DR KEGG; ecj:JW3262; -.
DR KEGG; eco:b3300; -.
DR PATRIC; fig|1411691.4.peg.3431; -.
DR EchoBASE; EB0759; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_2_6; -.
DR InParanoid; P0AGA2; -.
DR OMA; FAMWLGE; -.
DR PhylomeDB; P0AGA2; -.
DR BioCyc; EcoCyc:SECY; -.
DR BioCyc; MetaCyc:SECY; -.
DR EvolutionaryTrace; P0AGA2; -.
DR PRO; PR:P0AGA2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:CACAO.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0005048; F:signal sequence binding; IDA:EcoCyc.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006886; P:intracellular protein transport; IMP:EcoliWiki.
DR GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:EcoCyc.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:ComplexPortal.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:EcoCyc.
DR Gene3D; 1.10.3370.10; -; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..443
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131721"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 36..60
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 61..96
FT /note="Discontinuously helical; Name=2"
FT /evidence="ECO:0000250"
FT INTRAMEM 61..70
FT /note="Helical; Name=Helix 2A"
FT /evidence="ECO:0000305"
FT INTRAMEM 71..76
FT /evidence="ECO:0000305"
FT INTRAMEM 77..96
FT /note="Helical; Name=Helix 2B"
FT /evidence="ECO:0000305"
FT TOPO_DOM 97..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 132..164
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 179..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..200
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305"
FT TOPO_DOM 201..223
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..237
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305"
FT TOPO_DOM 238..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..287
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305"
FT TOPO_DOM 288..313
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 314..329
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305"
FT TOPO_DOM 330..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 381..395
FT /note="Helical; Name=9"
FT /evidence="ECO:0000305"
FT TOPO_DOM 396
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..413
FT /note="Helical; Name=10"
FT /evidence="ECO:0000305"
FT TOPO_DOM 414..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 40
FT /note="P->S: In secY100; temperature-sensitive."
FT MUTAGEN 60..74
FT /note="Missing: Some loss of viability, supports protein
FT translocation; strongly suppresses defective and missing
FT signal sequences; transient transmembrane channels open."
FT /evidence="ECO:0000269|PubMed:17531809,
FT ECO:0000269|PubMed:17531810"
FT MUTAGEN 65..70
FT /note="Missing: Grows almost as well as wild-type, supports
FT protein translocation; strongly suppresses defective and
FT missing signal sequences; transient transmembrane channels
FT open."
FT /evidence="ECO:0000269|PubMed:17531809,
FT ECO:0000269|PubMed:17531810"
FT MUTAGEN 67
FT /note="F->C: In prlA3; altered signal sequence interaction,
FT transient channel opening and closing in presence of
FT oxidant; massive ion flux when cross-linked to SecE C-120
FT mutation."
FT /evidence="ECO:0000269|PubMed:17531809"
FT MUTAGEN 167
FT /note="G->E: In secY100; temperature-sensitive."
FT MUTAGEN 240
FT /note="G->D: In secY24; temperature-sensitive at 42 degrees
FT Celsius, impairs interaction with SecE even at 30 degrees
FT in vitro."
FT /evidence="ECO:0000269|PubMed:8183945"
FT MUTAGEN 282
FT /note="S->R: In prlA401; altered signal sequence
FT interaction, transient transmembrane channels open."
FT MUTAGEN 286
FT /note="F->Y: In prlA4-1; altered signal sequence
FT interaction."
FT MUTAGEN 287
FT /note="P->L: In secY161; altered signal sequence
FT interaction."
FT MUTAGEN 290
FT /note="I->T: In secY121; altered signal sequence
FT interaction."
FT MUTAGEN 357
FT /note="R->H: In secY39; cold-sensitive."
FT MUTAGEN 363
FT /note="A->S: In secY40; cold-sensitive."
FT MUTAGEN 408
FT /note="I->N: In prlA4-2; altered signal sequence
FT interaction."
FT /evidence="ECO:0000269|PubMed:17531809"
FT MUTAGEN 424..443
FT /note="Missing: No longer complements secY24, a
FT temperature-sensitive secY mutation."
FT /evidence="ECO:0000269|PubMed:20855604"
FT HELIX 17..36
FT /evidence="ECO:0007829|PDB:5GAE"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:5GAE"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5GAE"
FT TURN 71..75
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 110..138
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 155..176
FT /evidence="ECO:0007829|PDB:5GAE"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5GAE"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:5GAE"
FT TURN 209..213
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 217..239
FT /evidence="ECO:0007829|PDB:5GAE"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:5GAE"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:5GAE"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:5GAE"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 315..336
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 360..394
FT /evidence="ECO:0007829|PDB:5GAE"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 404..426
FT /evidence="ECO:0007829|PDB:5GAE"
SQ SEQUENCE 443 AA; 48512 MW; 711CA63CD8809763 CRC64;
MAKQPGLDFQ SAKGGLGELK RRLLFVIGAL IVFRIGSFIP IPGIDAAVLA KLLEQQRGTI
IEMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTVVHP TLAEIKKEGE SGRRKISQYT
RYGTLVLAIF QSIGIATGLP NMPGMQGLVI NPGFAFYFTA VVSLVTGTMF LMWLGEQITE
RGIGNGISII IFAGIVAGLP PAIAHTIEQA RQGDLHFLVL LLVAVLVFAV TFFVVFVERG
QRRIVVNYAK RQQGRRVYAA QSTHLPLKVN MAGVIPAIFA SSIILFPATI ASWFGGGTGW
NWLTTISLYL QPGQPLYVLL YASAIIFFCF FYTALVFNPR ETADNLKKSG AFVPGIRPGE
QTAKYIDKVM TRLTLVGALY ITFICLIPEF MRDAMKVPFY FGGTSLLIVV VVIMDFMAQV
QTLMMSSQYE SALKKANLKG YGR
