SECA_ECOLI
ID SECA_ECOLI Reviewed; 901 AA.
AC P10408; P75642;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000305};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:1825804, ECO:0000269|PubMed:2542029, ECO:0000305|PubMed:2153463};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; Synonyms=azi, pea, prlD;
GN OrderedLocusNames=b0098, JW0096;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2841285; DOI=10.1128/jb.170.8.3404-3414.1988;
RA Schmidt M., Rollo E., Grodberg J., Oliver D.;
RT "Nucleotide sequence of the secA gene and secA(Ts) mutations preventing
RT protein export in Escherichia coli.";
RL J. Bacteriol. 170:3404-3414(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 TO
RP 737-738.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RC STRAIN=K12;
RX PubMed=2824434; DOI=10.1128/jb.169.12.5408-5415.1987;
RA Beall B., Lutkenhaus J.;
RT "Sequence analysis, transcriptional organization, and insertional
RT mutagenesis of the envA gene of Escherichia coli.";
RL J. Bacteriol. 169:5408-5415(1987).
RN [6]
RP FUNCTION.
RX PubMed=2846186; DOI=10.1016/0092-8674(88)90227-9;
RA Cabelli R.J., Chen L., Tai P.C., Oliver D.B.;
RT "SecA protein is required for secretory protein translocation into E. coli
RT membrane vesicles.";
RL Cell 55:683-692(1988).
RN [7]
RP ATP HYDROLYSIS, AND CATALYTIC ACTIVITY.
RX PubMed=2542029; DOI=10.1002/j.1460-2075.1989.tb03458.x;
RA Lill R., Cunningham K., Brundage L.A., Ito K., Oliver D., Wickner W.;
RT "SecA protein hydrolyzes ATP and is an essential component of the protein
RT translocation ATPase of Escherichia coli.";
RL EMBO J. 8:961-966(1989).
RN [8]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=2153463; DOI=10.1016/0092-8674(90)90742-w;
RA Lill R., Dowhan W., Wickner W.;
RT "The ATPase activity of SecA is regulated by acidic phospholipids, SecY,
RT and the leader and mature domains of precursor proteins.";
RL Cell 60:271-280(1990).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1825804; DOI=10.1016/0092-8674(91)90317-r;
RA Schiebel E., Driessen A.J., Hartl F.U., Wickner W.;
RT "Delta mu H+ and ATP function at different steps of the catalytic cycle of
RT preprotein translocase.";
RL Cell 64:927-939(1991).
RN [10]
RP FUNCTION.
RX PubMed=1830665; DOI=10.1073/pnas.88.15.6545;
RA Akimaru J., Matsuyama S., Tokuda H., Mizushima S.;
RT "Reconstitution of a protein translocation system containing purified SecY,
RT SecE, and SecA from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6545-6549(1991).
RN [11]
RP COFACTOR.
RX PubMed=10213615; DOI=10.1021/bi982818r;
RA Fekkes P., de Wit J.G., Boorsma A., Friesen R.H.E., Driessen A.J.M.;
RT "Zinc stabilizes the SecB binding site of SecA.";
RL Biochemistry 38:5111-5116(1999).
RN [12]
RP FUNCTION, AND REVIEW.
RX PubMed=10931320; DOI=10.1046/j.1365-2958.2000.01980.x;
RA Manting E.H., Driessen A.J.;
RT "Escherichia coli translocase: the unravelling of a molecular machine.";
RL Mol. Microbiol. 37:226-238(2000).
RN [13]
RP DIMER DISSOCIATION IN THE PRESENCE OF ACIDIC PHOSPHOLIPIDS, DETERGENTS, AND
RP SYNTHETIC SIGNAL PEPTIDES.
RX PubMed=12198149; DOI=10.1093/emboj/cdf471;
RA Or E., Navon A., Rapoport T.;
RT "Dissociation of the dimeric SecA ATPase during protein translocation
RT across the bacterial membrane.";
RL EMBO J. 21:4470-4479(2002).
RN [14]
RP ASSOCIATION OF MONOMER WITH SECYEG TRANSLOCATION COMPLEX.
RX PubMed=12941690; DOI=10.1093/emboj/cdg418;
RA Duong F.;
RT "Binding, activation and dissociation of the dimeric SecA ATPase at the
RT dimeric SecYEG translocase.";
RL EMBO J. 22:4375-4384(2003).
RN [15]
RP ACIDIC PHOSPHOLIPIDS, SYNTHETIC SIGNAL PEPTIDES, AND OLIGOMERIZATION STATE
RP OF SECA.
RX PubMed=12403785; DOI=10.1074/jbc.m205992200;
RA Benach J., Chou Y.T., Fak J.J., Itkin A., Nicolae D.D., Smith P.C.,
RA Wittrock G., Floyd D.L., Golsaz C.M., Gierasch L.M., Hunt J.F.;
RT "Phospholipid-induced monomerization and signal-peptide-induced
RT oligomerization of SecA.";
RL J. Biol. Chem. 278:3628-3638(2003).
RN [16]
RP NUCLEOTIDE TURNOVER, AND OLIGOMERIZATION STATE OF SECA.
RX PubMed=12946344; DOI=10.1016/s0022-2836(03)00840-4;
RA Bu Z., Wang L., Kendall D.A.;
RT "Nucleotide binding induces changes in the oligomeric state and
RT conformation of Sec A in a lipid environment: a small-angle neutron-
RT scattering study.";
RL J. Mol. Biol. 332:23-30(2003).
RN [17]
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 [18]
RP INTERACTION WITH SECY.
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 [19]
RP CONTROL OF ATPASE ACTIVITY.
RX PubMed=17525736; DOI=10.1038/sj.emboj.7601721;
RA Karamanou S., Gouridis G., Papanikou E., Sianidis G., Gelis I.,
RA Keramisanou D., Vrontou E., Kalodimos C.G., Economou A.;
RT "Preprotein-controlled catalysis in the helicase motor of SecA.";
RL EMBO J. 26:2904-2914(2007).
RN [20]
RP STRUCTURE BY NMR OF 880-901.
RX PubMed=15488768; DOI=10.1016/j.bbapap.2004.08.012;
RA Matousek W.M., Alexandrescu A.T.;
RT "NMR structure of the C-terminal domain of SecA in the free state.";
RL Biochim. Biophys. Acta 1702:163-171(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-861 AS A DIMERIC APOPROTEIN, AND
RP AS A NUCLEOTIDE-BOUND DIMER.
RX PubMed=17229438; DOI=10.1016/j.jmb.2006.12.049;
RA Papanikolau Y., Papadovasilaki M., Ravelli R.B.G., McCarthy A.A.,
RA Cusack S., Economou A., Petratos K.;
RT "Structure of dimeric SecA, the Escherichia coli preprotein translocase
RT motor.";
RL J. Mol. Biol. 366:1545-1557(2007).
RN [22]
RP REVIEW OF PROTEIN SECRETION CONTROL OF SECA EXPRESSION.
RX PubMed=15063851; DOI=10.1016/j.mib.2004.01.001;
RA Nakatogawa H., Murakami A., Ito K.;
RT "Control of SecA and SecM translation by protein secretion.";
RL Curr. Opin. Microbiol. 7:145-150(2004).
RN [23]
RP REVIEW OF PROTEIN SECRETION.
RX PubMed=17938627; DOI=10.1038/nrmicro1771;
RA Papanikou E., Karamanou S., Economou A.;
RT "Bacterial protein secretion through the translocase nanomachine.";
RL Nat. Rev. Microbiol. 5:839-851(2007).
CC -!- FUNCTION: Required for protein export, interacts with the SecYEG
CC preprotein conducting channel. SecA has a central role in coupling the
CC hydrolysis of ATP to the transfer of proteins into and across the cell
CC membrane, serving both as a receptor for the preprotein-SecB complex
CC and as an ATP-driven molecular motor driving the stepwise translocation
CC of polypeptide chains across the membrane.
CC {ECO:0000269|PubMed:10931320, ECO:0000269|PubMed:15140892,
CC ECO:0000269|PubMed:1825804, ECO:0000269|PubMed:1830665,
CC ECO:0000269|PubMed:2846186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01382, ECO:0000269|PubMed:1825804,
CC ECO:0000269|PubMed:2542029, ECO:0000305|PubMed:2153463};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382,
CC ECO:0000269|PubMed:10213615};
CC Note=Binds 1 zinc ion per subunit. Zinc is required for binding of the
CC SecB chaperone to the extreme C-terminus of SecA.
CC {ECO:0000269|PubMed:10213615};
CC -!- ACTIVITY REGULATION: The translocation ATPase activity is stimulated by
CC SecY and a precursor protein such as proOmpA.
CC {ECO:0000269|PubMed:2153463}.
CC -!- SUBUNIT: Monomer and homodimer; probably dimeric in the cytoplasm. It
CC is not yet clear whether the form that functions in protein insertion
CC is monomeric or dimeric. Part of the essential protein translocation
CC apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-
CC YajC and YidC. Makes direct contact with SecY.
CC -!- INTERACTION:
CC P10408; P02943: lamB; NbExp=3; IntAct=EBI-543213, EBI-371309;
CC P10408; P0A910: ompA; NbExp=2; IntAct=EBI-543213, EBI-371347;
CC P10408; P00634: phoA; NbExp=3; IntAct=EBI-543213, EBI-552958;
CC P10408; P10408: secA; NbExp=3; IntAct=EBI-543213, EBI-543213;
CC P10408; P0AG86: secB; NbExp=6; IntAct=EBI-543213, EBI-555877;
CC P10408; P0AG96: secE; NbExp=2; IntAct=EBI-543213, EBI-6404267;
CC P10408; P0AG99: secG; NbExp=3; IntAct=EBI-543213, EBI-6404248;
CC P10408; P0AGA2: secY; NbExp=6; IntAct=EBI-543213, EBI-761422;
CC P10408; P0A8Z3: ybgC; NbExp=2; IntAct=EBI-543213, EBI-543276;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- INDUCTION: Repressed under conditions of excess protein secretion
CC capacity and derepressed when protein secretion becomes limiting. This
CC is regulated by SecM. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- DISRUPTION PHENOTYPE: Essential. Leads to loss of translocation of
CC lipoproteins Lpp and BRP. {ECO:0000269|PubMed:15140892}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382, 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; M20791; AAA24619.1; -; Genomic_DNA.
DR EMBL; M19211; AAA83851.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38875.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73209.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96666.2; -; Genomic_DNA.
DR PIR; B64732; BVECCA.
DR RefSeq; NP_414640.1; NC_000913.3.
DR RefSeq; WP_000905789.1; NZ_STEB01000010.1.
DR PDB; 1TM6; NMR; -; A=880-901.
DR PDB; 2FSF; X-ray; 2.00 A; A/B=9-861.
DR PDB; 2FSG; X-ray; 2.20 A; A/B=9-861.
DR PDB; 2FSH; X-ray; 2.00 A; A/B=9-861.
DR PDB; 2FSI; X-ray; 2.11 A; A/B=9-861.
DR PDB; 2VDA; NMR; -; A=9-836.
DR PDB; 3BXZ; X-ray; 3.00 A; A/B=6-609.
DR PDB; 6GOX; X-ray; 3.50 A; A=13-834.
DR PDBsum; 1TM6; -.
DR PDBsum; 2FSF; -.
DR PDBsum; 2FSG; -.
DR PDBsum; 2FSH; -.
DR PDBsum; 2FSI; -.
DR PDBsum; 2VDA; -.
DR PDBsum; 3BXZ; -.
DR PDBsum; 6GOX; -.
DR AlphaFoldDB; P10408; -.
DR SASBDB; P10408; -.
DR SMR; P10408; -.
DR BioGRID; 4261117; 260.
DR BioGRID; 849222; 4.
DR DIP; DIP-10840N; -.
DR IntAct; P10408; 86.
DR MINT; P10408; -.
DR STRING; 511145.b0098; -.
DR ChEMBL; CHEMBL4662929; -.
DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family.
DR jPOST; P10408; -.
DR PaxDb; P10408; -.
DR PRIDE; P10408; -.
DR EnsemblBacteria; AAC73209; AAC73209; b0098.
DR EnsemblBacteria; BAB96666; BAB96666; BAB96666.
DR GeneID; 66671612; -.
DR GeneID; 944821; -.
DR KEGG; ecj:JW0096; -.
DR KEGG; eco:b0098; -.
DR PATRIC; fig|1411691.4.peg.2182; -.
DR EchoBASE; EB0929; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_6; -.
DR InParanoid; P10408; -.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; P10408; -.
DR BioCyc; EcoCyc:SECA; -.
DR BRENDA; 7.4.2.5; 2026.
DR EvolutionaryTrace; P10408; -.
DR PRO; PR:P10408; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070678; F:preprotein binding; IDA:EcoCyc.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IMP:EcoCyc.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IMP:EcoliWiki.
DR GO; GO:0015031; P:protein transport; IMP:EcoliWiki.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:EcoCyc.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004027; SEC_C_motif.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR PANTHER; PTHR30612; PTHR30612; 1.
DR Pfam; PF02810; SEC-C; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 1.
DR TIGRFAMs; TIGR00963; secA; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport; Zinc.
FT CHAIN 1..901
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109585"
FT REGION 859..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 105..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT CONFLICT 19
FT /note="R -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 737..738
FT /note="ER -> DG (in Ref. 1; AAA24619 and 2; CAA38875)"
FT /evidence="ECO:0000305"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3BXZ"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 215..220
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:2FSI"
FT TURN 239..244
FT /evidence="ECO:0007829|PDB:2FSI"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:2VDA"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2FSI"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2VDA"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6GOX"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6GOX"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6GOX"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6GOX"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:2VDA"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:2VDA"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:2VDA"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:6GOX"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6GOX"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 431..446
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 459..471
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:2VDA"
FT HELIX 484..492
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:3BXZ"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 519..525
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2VDA"
FT HELIX 533..550
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 553..560
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 565..572
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 582..589
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:3BXZ"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:2VDA"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 605..610
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:6GOX"
FT HELIX 621..668
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 673..689
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 703..714
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 720..726
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:2VDA"
FT HELIX 732..754
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 756..787
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 788..790
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:2FSF"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 799..801
FT /evidence="ECO:0007829|PDB:2FSF"
FT HELIX 802..828
FT /evidence="ECO:0007829|PDB:2FSF"
FT TURN 884..887
FT /evidence="ECO:0007829|PDB:1TM6"
FT STRAND 889..891
FT /evidence="ECO:0007829|PDB:1TM6"
FT HELIX 892..896
FT /evidence="ECO:0007829|PDB:1TM6"
SQ SEQUENCE 901 AA; 102023 MW; 683D66DD4305DBC2 CRC64;
MLIKLLTKVF GSRNDRTLRR MRKVVNIINA MEPEMEKLSD EELKGKTAEF RARLEKGEVL
ENLIPEAFAV VREASKRVFG MRHFDVQLLG GMVLNERCIA EMRTGEGKTL TATLPAYLNA
LTGKGVHVVT VNDYLAQRDA ENNRPLFEFL GLTVGINLPG MPAPAKREAY AADITYGTNN
EYGFDYLRDN MAFSPEERVQ RKLHYALVDE VDSILIDEAR TPLIISGPAE DSSEMYKRVN
KIIPHLIRQE KEDSETFQGE GHFSVDEKSR QVNLTERGLV LIEELLVKEG IMDEGESLYS
PANIMLMHHV TAALRAHALF TRDVDYIVKD GEVIIVDEHT GRTMQGRRWS DGLHQAVEAK
EGVQIQNENQ TLASITFQNY FRLYEKLAGM TGTADTEAFE FSSIYKLDTV VVPTNRPMIR
KDLPDLVYMT EAEKIQAIIE DIKERTAKGQ PVLVGTISIE KSELVSNELT KAGIKHNVLN
AKFHANEAAI VAQAGYPAAV TIATNMAGRG TDIVLGGSWQ AEVAALENPT AEQIEKIKAD
WQVRHDAVLE AGGLHIIGTE RHESRRIDNQ LRGRSGRQGD AGSSRFYLSM EDALMRIFAS
DRVSGMMRKL GMKPGEAIEH PWVTKAIANA QRKVESRNFD IRKQLLEYDD VANDQRRAIY
SQRNELLDVS DVSETINSIR EDVFKATIDA YIPPQSLEEM WDIPGLQERL KNDFDLDLPI
AEWLDKEPEL HEETLRERIL AQSIEVYQRK EEVVGAEMMR HFEKGVMLQT LDSLWKEHLA
AMDYLRQGIH LRGYAQKDPK QEYKRESFSM FAAMLESLKY EVISTLSKVQ VRMPEEVEEL
EQQRRMEAER LAQMQQLSHQ DDDSAAAAAL AAQTGERKVG RNDPCPCGSG KKYKQCHGRL
Q
