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Entry: CYDB_ECOLI
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Original site: CYDB_ECOLI 
ID   CYDB_ECOLI              Reviewed;         379 AA.
AC   P0ABK2; P11027;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Cytochrome bd-I ubiquinol oxidase subunit 2;
DE            EC=7.1.1.7 {ECO:0000269|PubMed:1850294};
DE   AltName: Full=Cytochrome bd-I oxidase subunit II;
DE   AltName: Full=Cytochrome d ubiquinol oxidase subunit II;
GN   Name=cydB; Synonyms=cyd-2; OrderedLocusNames=b0734, JW0723;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2843510; DOI=10.1016/s0021-9258(18)37682-8;
RA   Green G.N., Fang H., Lin R.-J., Newton G., Mather M., Georgiou C.D.,
RA   Gennis R.B.;
RT   "The nucleotide sequence of the cyd locus encoding the two subunits of the
RT   cytochrome d terminal oxidase complex of Escherichia coli.";
RL   J. Biol. Chem. 263:13138-13143(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
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 1-6, FORMYLATION AT MET-1, AND SUBUNIT.
RC   STRAIN=MR43L/F152;
RX   PubMed=3281937; DOI=10.1016/s0021-9258(18)60705-7;
RA   Miller M.J., Hermodson M., Gennis R.B.;
RT   "The active form of the cytochrome d terminal oxidase complex of
RT   Escherichia coli is a heterodimer containing one copy of each of the two
RT   subunits.";
RL   J. Biol. Chem. 263:5235-5240(1988).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 361-379.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Kim K., Allen E., Araujo R., Aparicio A.M., Botstein D., Cherry M.,
RA   Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Komp C.,
RA   Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP   COFACTOR, SUBUNIT, AND INDUCTION.
RC   STRAIN=MR43L/F152;
RX   PubMed=6307994; DOI=10.1016/s0021-9258(17)44645-x;
RA   Miller M.J., Gennis R.B.;
RT   "The purification and characterization of the cytochrome d terminal oxidase
RT   complex of the Escherichia coli aerobic respiratory chain.";
RL   J. Biol. Chem. 258:9159-9165(1983).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=3013298; DOI=10.1021/bi00357a002;
RA   Green G.N., Lorence R.M., Gennis R.B.;
RT   "Specific overproduction and purification of the cytochrome b558 component
RT   of the cytochrome d complex from Escherichia coli.";
RL   Biochemistry 25:2309-2314(1986).
RN   [9]
RP   COFACTOR.
RC   STRAIN=MR43L/F152;
RX   PubMed=3013299; DOI=10.1021/bi00357a003;
RA   Lorence R.M., Koland J.G., Gennis R.B.;
RT   "Coulometric and spectroscopic analysis of the purified cytochrome d
RT   complex of Escherichia coli: evidence for the identification of 'cytochrome
RT   a1' as cytochrome b595.";
RL   Biochemistry 25:2314-2321(1986).
RN   [10]
RP   TOPOLOGY.
RX   PubMed=3138232; DOI=10.1016/s0021-9258(18)37681-6;
RA   Georgiou C.D., Dueweke T.J., Gennis R.B.;
RT   "Beta-galactosidase gene fusions as probes for the cytoplasmic regions of
RT   subunits I and II of the membrane-bound cytochrome d terminal oxidase from
RT   Escherichia coli.";
RL   J. Biol. Chem. 263:13130-13137(1988).
RN   [11]
RP   COFACTOR, AND MUTAGENESIS OF HIS-56; HIS-197; HIS-237 AND HIS-376.
RX   PubMed=2656671; DOI=10.1016/s0021-9258(18)83145-3;
RA   Fang H., Lin R.J., Gennis R.B.;
RT   "Location of heme axial ligands in the cytochrome d terminal oxidase
RT   complex of Escherichia coli determined by site-directed mutagenesis.";
RL   J. Biol. Chem. 264:8026-8032(1989).
RN   [12]
RP   CATALYTIC ACTIVITY.
RX   PubMed=1850294; DOI=10.1021/bi00230a019;
RA   Puustinen A., Finel M., Haltia T., Gennis R.B., Wikstroem M.;
RT   "Properties of the two terminal oxidases of Escherichia coli.";
RL   Biochemistry 30:3936-3942(1991).
RN   [13]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=15013751; DOI=10.1016/s0014-5793(04)00125-5;
RA   Zhang J., Barquera B., Gennis R.B.;
RT   "Gene fusions with beta-lactamase show that subunit I of the cytochrome bd
RT   quinol oxidase from E. coli has nine transmembrane helices with the O2
RT   reactive site near the periplasmic surface.";
RL   FEBS Lett. 561:58-62(2004).
RN   [14]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BL21-DE3;
RX   PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA   Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA   von Heijne G., Daley D.O.;
RT   "Protein complexes of the Escherichia coli cell envelope.";
RL   J. Biol. Chem. 280:34409-34419(2005).
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   FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=19542282; DOI=10.1128/jb.00562-09;
RA   Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.;
RT   "Respiration of Escherichia coli can be fully uncoupled via the
RT   nonelectrogenic terminal cytochrome bd-II oxidase.";
RL   J. Bacteriol. 191:5510-5517(2009).
RN   [17]
RP   ROLE IN HYDROXYUREA RESISTANCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA   Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA   Walker G.C.;
RT   "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT   coli.";
RL   Mol. Cell 36:845-860(2009).
RN   [18]
RP   FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=21987791; DOI=10.1073/pnas.1108217108;
RA   Borisov V.B., Murali R., Verkhovskaya M.L., Bloch D.A., Han H.,
RA   Gennis R.B., Verkhovsky M.I.;
RT   "Aerobic respiratory chain of Escherichia coli is not allowed to work in
RT   fully uncoupled mode.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:17320-17324(2011).
RN   [19]
RP   PROBABLE INTERACTION WITH CYDX, POSSIBLE INTERACTION WITH APPX, SUBUNIT,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=23749980; DOI=10.1128/jb.00324-13;
RA   Vanorsdel C.E., Bhatt S., Allen R.J., Brenner E.P., Hobson J.J., Jamil A.,
RA   Haynes B.M., Genson A.M., Hemm M.R.;
RT   "The Escherichia coli CydX protein is a member of the CydAB cytochrome bd
RT   oxidase complex and is required for cytochrome bd oxidase activity.";
RL   J. Bacteriol. 195:3640-3650(2013).
RN   [20]
RP   REVIEW.
RX   PubMed=21756872; DOI=10.1016/j.bbabio.2011.06.016;
RA   Borisov V.B., Gennis R.B., Hemp J., Verkhovsky M.I.;
RT   "The cytochrome bd respiratory oxygen reductases.";
RL   Biochim. Biophys. Acta 1807:1398-1413(2011).
CC   -!- FUNCTION: A terminal oxidase that produces a proton motive force by the
CC       vectorial transfer of protons across the inner membrane. It is the
CC       component of the aerobic respiratory chain of E.coli that predominates
CC       when cells are grown at low aeration. Generates a proton motive force
CC       using protons and electrons from opposite sides of the membrane to
CC       generate H(2)O, transferring 1 proton/electron.
CC       {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791,
CC       ECO:0000269|PubMed:6307994}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4
CC         H(+)(out) + 2 H2O(in); Xref=Rhea:RHEA:40527, Rhea:RHEA-COMP:9565,
CC         Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.7;
CC         Evidence={ECO:0000269|PubMed:1850294};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013299,
CC         ECO:0000269|PubMed:6307994};
CC       Note=Binds 1 protoheme IX center (heme b595, originally called
CC       cytochrome a1) per heterodimer, in conjunction with CydA.
CC       {ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013299,
CC       ECO:0000269|PubMed:6307994};
CC   -!- COFACTOR:
CC       Name=heme d cis-diol; Xref=ChEBI:CHEBI:62814;
CC         Evidence={ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013299,
CC         ECO:0000269|PubMed:6307994};
CC       Note=Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in
CC       conjunction with CydA. {ECO:0000269|PubMed:2656671,
CC       ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994};
CC   -!- ACTIVITY REGULATION: 90% inhibited by cyanide and 2-heptyl-4-
CC       hydroxyquinoline N-oxide, at 1 mM and 40 uM respectively.
CC       {ECO:0000269|PubMed:6307994}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.1 mM for ubiquinol-1 {ECO:0000269|PubMed:6307994};
CC         KM=0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine
CC         {ECO:0000269|PubMed:6307994};
CC         KM=0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine
CC         {ECO:0000269|PubMed:6307994};
CC         Vmax=383 umol/min/mg enzyme for ubiquinol-1
CC         {ECO:0000269|PubMed:6307994};
CC         Vmax=270 umol/min/mg enzyme for 2,3,5,6-tetramethyl-p-
CC         phenylenediamine {ECO:0000269|PubMed:6307994};
CC         Vmax=126 umol/min/mg enzyme for N,N,N',N'-tetramethyl-p-
CC         phenylenediamine {ECO:0000269|PubMed:6307994};
CC         Note=pH 7.0, 37 degrees Celsius.;
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBUNIT: Heterodimer of subunits I and II. Probably interacts with
CC       CydX, and overexpressed AppX. {ECO:0000269|PubMed:16079137,
CC       ECO:0000269|PubMed:23749980, ECO:0000269|PubMed:3281937,
CC       ECO:0000269|PubMed:6307994}.
CC   -!- INTERACTION:
CC       P0ABK2; P0ABJ9: cydA; NbExp=5; IntAct=EBI-1213195, EBI-906928;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15013751,
CC       ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}. Note=The
CC       displayed topology is based on (PubMed:15013751) not the large scale
CC       studies (PubMed:15919996). {ECO:0000269|PubMed:15013751,
CC       ECO:0000269|PubMed:15919996}.
CC   -!- INDUCTION: Under conditions of low aeration, in stationary phase (at
CC       protein level). {ECO:0000269|PubMed:6307994}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- DISRUPTION PHENOTYPE: Loss of cytochrome b595 and d from enzyme
CC       preparations (PubMed:3013298). A double cydA/cydB deletion shows
CC       increased sensitivity to reductant (beta-mercapoethanol)
CC       (PubMed:23749980). Greatly increased resistance to hydroxyurea,
CC       probably due to decreased OH radical formation as an electron transport
CC       chain is disrupted (PubMed:20005847). {ECO:0000269|PubMed:19542282,
CC       ECO:0000269|PubMed:20005847, ECO:0000269|PubMed:21987791,
CC       ECO:0000269|PubMed:23749980, ECO:0000269|PubMed:3013298}.
CC   -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC       family. {ECO:0000305}.
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DR   EMBL; J03939; AAA18805.1; -; Unassigned_DNA.
DR   EMBL; U00096; AAC73828.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35400.1; -; Genomic_DNA.
DR   EMBL; U30934; AAA74397.1; -; Genomic_DNA.
DR   PIR; B28940; B28940.
DR   RefSeq; NP_415262.1; NC_000913.3.
DR   RefSeq; WP_000568275.1; NZ_STEB01000035.1.
DR   PDB; 6RKO; EM; 2.68 A; B=1-379.
DR   PDB; 6RX4; EM; 3.30 A; B=1-379.
DR   PDBsum; 6RKO; -.
DR   PDBsum; 6RX4; -.
DR   AlphaFoldDB; P0ABK2; -.
DR   EMDB; EMD-10049; -.
DR   EMDB; EMD-4908; -.
DR   SMR; P0ABK2; -.
DR   BioGRID; 4263540; 447.
DR   ComplexPortal; CPX-268; Cytochrome bd-I ubiquinol oxidase complex.
DR   IntAct; P0ABK2; 2.
DR   MINT; P0ABK2; -.
DR   STRING; 511145.b0734; -.
DR   TCDB; 3.D.4.3.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR   jPOST; P0ABK2; -.
DR   PaxDb; 511145-b0734; -.
DR   EnsemblBacteria; AAC73828; AAC73828; b0734.
DR   GeneID; 75205565; -.
DR   GeneID; 945347; -.
DR   KEGG; ecj:JW0723; -.
DR   KEGG; eco:b0734; -.
DR   PATRIC; fig|1411691.4.peg.1539; -.
DR   EchoBASE; EB0171; -.
DR   eggNOG; COG1294; Bacteria.
DR   HOGENOM; CLU_049294_0_0_6; -.
DR   InParanoid; P0ABK2; -.
DR   OMA; FLWGVAF; -.
DR   OrthoDB; 9776710at2; -.
DR   PhylomeDB; P0ABK2; -.
DR   BioCyc; EcoCyc:CYDB-MONOMER; -.
DR   BioCyc; MetaCyc:CYDB-MONOMER; -.
DR   BRENDA; 7.1.1.7; 2026.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:P0ABK2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0070069; C:cytochrome complex; IDA:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IDA:EcoCyc.
DR   GO; GO:0019646; P:aerobic electron transport chain; IDA:EcoCyc.
DR   GO; GO:0006119; P:oxidative phosphorylation; NAS:ComplexPortal.
DR   InterPro; IPR003317; Cyt-d_oxidase_su2.
DR   NCBIfam; TIGR00203; cydB; 1.
DR   PANTHER; PTHR43141:SF5; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR43141; CYTOCHROME BD2 SUBUNIT II; 1.
DR   Pfam; PF02322; Cyt_bd_oxida_II; 1.
DR   PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane;
KW   Direct protein sequencing; Electron transport; Formylation; Heme; Iron;
KW   Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..379
FT                   /note="Cytochrome bd-I ubiquinol oxidase subunit 2"
FT                   /id="PRO_0000183925"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        29..79
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        80..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        100..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        123..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        143..164
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        185..205
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        206..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        226..262
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        263..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        283..292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        293..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        313..336
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        337..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        357..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:3281937"
FT   MUTAGEN         56
FT                   /note="H->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:2656671"
FT   MUTAGEN         197
FT                   /note="H->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:2656671"
FT   MUTAGEN         237
FT                   /note="H->L,R: No effect."
FT                   /evidence="ECO:0000269|PubMed:2656671"
FT   MUTAGEN         376
FT                   /note="H->P: No effect."
FT                   /evidence="ECO:0000269|PubMed:2656671"
FT   HELIX           4..25
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           27..35
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           43..53
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           62..74
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           76..85
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           87..97
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           99..106
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           113..141
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:6RX4"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           167..191
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           194..223
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   STRAND          227..231
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:6RX4"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:6RX4"
FT   STRAND          248..252
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           257..261
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           263..266
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           267..284
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           288..310
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   STRAND          313..315
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   TURN            327..329
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           334..361
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   HELIX           368..373
FT                   /evidence="ECO:0007829|PDB:6RKO"
FT   TURN            374..377
FT                   /evidence="ECO:0007829|PDB:6RKO"
SQ   SEQUENCE   379 AA;  42453 MW;  A3775AC95F713D0C CRC64;
     MIDYEVLRFI WWLLVGVLLI GFAVTDGFDM GVGMLTRFLG RNDTERRIMI NSIAPHWDGN
     QVWLITAGGA LFAAWPMVYA AAFSGFYVAM ILVLASLFFR PVGFDYRSKI EETRWRNMWD
     WGIFIGSFVP PLVIGVAFGN LLQGVPFNVD EYLRLYYTGN FFQLLNPFGL LAGVVSVGMI
     ITQGATYLQM RTVGELHLRT RATAQVAALV TLVCFALAGV WVMYGIDGYV VKSTMDHYAA
     SNPLNKEVVR EAGAWLVNFN NTPILWAIPA LGVVLPLLTI LTARMDKAAW AFVFSSLTLA
     CIILTAGIAM FPFVMPSSTM MNASLTMWDA TSSQLTLNVM TWVAVVLVPI ILLYTAWCYW
     KMFGRITKED IERNTHSLY
//
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