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 03-AUG-2022, entry version 125.
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; Proteobacteria; 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 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; P0ABK2; -.
DR PRIDE; P0ABK2; -.
DR EnsemblBacteria; AAC73828; AAC73828; b0734.
DR EnsemblBacteria; BAA35400; BAA35400; BAA35400.
DR GeneID; 66670997; -.
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 PhylomeDB; P0ABK2; -.
DR BioCyc; EcoCyc:CYDB-MON; -.
DR BioCyc; MetaCyc:CYDB-MON; -.
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:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
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; IC:ComplexPortal.
DR InterPro; IPR003317; Cyt-d_oxidase_su2.
DR PANTHER; PTHR43141; PTHR43141; 1.
DR Pfam; PF02322; Cyt_bd_oxida_II; 1.
DR PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1.
DR TIGRFAMs; TIGR00203; cydB; 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
