BACR_HALSA
ID BACR_HALSA Reviewed; 262 AA.
AC P02945; Q9HPU5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Bacteriorhodopsin;
DE Short=BR;
DE AltName: Full=Bacterioopsin;
DE Short=BO;
DE Flags: Precursor;
GN Name=bop; OrderedLocusNames=VNG_1467G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R1 / S9;
RX PubMed=12049093; DOI=10.1073/pnas.78.11.6744;
RA Dunn R.J., McCoy J., Simsek M., Majumdar A., Chang S.H., RajBhandary U.L.,
RA Khorana H.G.;
RT "The bacteriorhodopsin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:6744-6748(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6327180; DOI=10.1101/sqb.1983.048.01.088;
RA Dunn R.J., Hackett N.R., Huang K.-S., Jones S., Khorana H.G., Lee D.-S.,
RA Liao M.-J., Lo K.-M., McCoy J., Noguchi S., Radhakrishnan R.,
RA RajBhandary U.L.;
RT "Studies on the light-transducing pigment bacteriorhodopsin.";
RL Cold Spring Harb. Symp. Quant. Biol. 48:853-862(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SG1;
RX PubMed=8478333; DOI=10.1128/jb.175.9.2720-2726.1993;
RA Soppa J., Duschl J., Oesterhelt D.;
RT "Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate
RT Halobacterium sp. strain SG1: three new members of a growing family.";
RL J. Bacteriol. 175:2720-2726(1993).
RN [4]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TOPOLOGY, AND RETINAL BINDING.
RX PubMed=6706999; DOI=10.1016/s0021-9258(17)43028-6;
RA Seehra J.S., Khorana H.G.;
RT "Bacteriorhodopsin precursor. Characterization and its integration into the
RT purple membrane.";
RL J. Biol. Chem. 259:4187-4193(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [6]
RP PROTEIN SEQUENCE OF 14-261.
RA Ovchinnikov Y.A., Abdulaev N.G., Feigina M.Y., Kiselev A.V., Lobanov N.A.,
RA Nasimov I.V.;
RT "The amino acid sequence of bacteriorhodopsin.";
RL Bioorg. Khim. 4:1573-1574(1978).
RN [7]
RP PROTEIN SEQUENCE OF 14-261.
RX PubMed=291920; DOI=10.1073/pnas.76.10.5046;
RA Khorana H.G., Gerber G.E., Herlihy W.C., Gray C.P., Anderegg R.J.,
RA Nihei K., Biemann K.;
RT "Amino acid sequence of bacteriorhodopsin.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:5046-5050(1979).
RN [8]
RP PROTEIN SEQUENCE OF 14-248, AND PYROGLUTAMATE FORMATION AT GLN-14.
RX PubMed=9541408; DOI=10.1002/pro.5560070325;
RA Ball L.E., Oatis J.E. Jr., Dharmasiri K., Busman M., Wang J., Cowden L.B.,
RA Galijatovic A., Chen N., Crouch R.K., Knapp D.R.;
RT "Mass spectrometric analysis of integral membrane proteins: application to
RT complete mapping of bacteriorhodopsins and rhodopsin.";
RL Protein Sci. 7:758-764(1998).
RN [9]
RP RETINAL-BINDING SITE.
RX PubMed=6794028; DOI=10.1073/pnas.78.7.4068;
RA Katre N.V., Wolber P.K., Stoeckenius W., Stroud R.M.;
RT "Attachment site(s) of retinal in bacteriorhodopsin.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4068-4072(1981).
RN [10]
RP MASS SPECTROMETRY.
RX PubMed=9655347; DOI=10.1002/pro.5560070619;
RA Whitelegge J.P., Gundersen C.B., Faull K.F.;
RT "Electrospray-ionization mass spectrometry of intact intrinsic membrane
RT proteins.";
RL Protein Sci. 7:1423-1430(1998).
RN [11]
RP STRUCTURE BY NEUTRON DIFFRACTION, SUBUNIT, AND TOPOLOGY.
RX PubMed=2614846; DOI=10.1016/0022-2836(89)90111-3;
RA Popot J.-L., Engleman D.M., Gurel O., Zaccai G.;
RT "Tertiary structure of bacteriorhodopsin. Positions and orientations of
RT helices A and B in the structural map determined by neutron diffraction.";
RL J. Mol. Biol. 210:829-847(1989).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL.
RX PubMed=2359127; DOI=10.1016/s0022-2836(05)80271-2;
RA Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E.,
RA Downing K.H.;
RT "Model for the structure of bacteriorhodopsin based on high-resolution
RT electron cryo-microscopy.";
RL J. Mol. Biol. 213:899-929(1990).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL.
RX PubMed=8676377; DOI=10.1006/jmbi.1996.0328;
RA Grigorieff N., Ceska T.A., Downing K.H., Baldwin J.M., Henderson R.;
RT "Electron-crystallographic refinement of the structure of
RT bacteriorhodopsin.";
RL J. Mol. Biol. 259:393-421(1996).
RN [14]
RP STRUCTURE BY NMR OF 176-244.
RX PubMed=1606953; DOI=10.1111/j.1432-1033.1992.tb16972.x;
RA Barsukov I.L., Nolde D.E., Lomize A.L., Arseniev A.S.;
RT "Three-dimensional structure of proteolytic fragment 163-231 of
RT bacterioopsin determined from nuclear magnetic resonance data in
RT solution.";
RL Eur. J. Biochem. 206:665-672(1992).
RN [15]
RP STRUCTURE BY NMR OF 1-231.
RX PubMed=1332860; DOI=10.1111/j.1432-1033.1992.tb17412.x;
RA Orekhov V.Y., Abdulaeva G.V., Musina L.Y., Arseniev A.S.;
RT "1H-15N-NMR studies of bacteriorhodopsin Halobacterium halobium.
RT Conformational dynamics of the four-helical bundle.";
RL Eur. J. Biochem. 210:223-229(1992).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 15-244.
RX PubMed=9296502; DOI=10.1038/38323;
RA Kimura Y., Vassylyev D.G., Miyazawa A., Kidera A., Matsushima M.,
RA Mitsuoka K., Murata K., Hirai T., Fujiyoshi Y.;
RT "Surface of bacteriorhodopsin revealed by high-resolution electron
RT crystallography.";
RL Nature 389:206-211(1997).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, SUBUNIT, AND TOPOLOGY.
RX PubMed=9287223; DOI=10.1126/science.277.5332.1676;
RA Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M.;
RT "X-ray structure of bacteriorhodopsin at 2.5-A from microcrystals grown in
RT lipidic cubic phases.";
RL Science 277:1676-1681(1997).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, SUBUNIT, AND TOPOLOGY.
RX PubMed=9751724; DOI=10.1073/pnas.95.20.11673;
RA Essen L.-O., Siegert R., Lehmann W.D., Oesterhelt D.;
RT "Lipid patches in membrane protein oligomers: crystal structure of the
RT bacteriorhodopsin-lipid complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11673-11678(1998).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, SUBUNIT, AND TOPOLOGY.
RX PubMed=9632391; DOI=10.1126/science.280.5371.1934;
RA Luecke H., Richter H.-T., Lanyi J.K.;
RT "Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom
RT resolution.";
RL Science 280:1934-1937(1998).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-244 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, SUBUNIT, AND TOPOLOGY.
RX PubMed=10452895; DOI=10.1006/jmbi.1999.3027;
RA Luecke H., Schobert B., Richter H.-T., Cartailler J.-P., Lanyi J.K.;
RT "Structure of bacteriorhodopsin at 1.55-A resolution.";
RL J. Mol. Biol. 291:899-911(1999).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, AND TOPOLOGY.
RX PubMed=10548112; DOI=10.1038/44623;
RA Edman K., Nollert P., Royant A., Belrhali H., Pebay-Peyroula E., Hajdu J.,
RA Neutze R., Landau E.M.;
RT "High-resolution X-ray structure of an early intermediate in the
RT bacteriorhodopsin photocycle.";
RL Nature 401:822-826(1999).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, AND TOPOLOGY.
RX PubMed=10467143; DOI=10.1016/s0969-2126(99)80118-x;
RA Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P.,
RA Landau E.M., Pebay-Peyroula E.;
RT "Protein, lipid and water organization in bacteriorhodopsin crystals: a
RT molecular view of the purple membrane at 1.9 A resolution.";
RL Structure 7:909-917(1999).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-245 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, FUNCTION, AND TOPOLOGY.
RX PubMed=10903866; DOI=10.1006/jmbi.2000.3884;
RA Luecke H., Schobert B., Cartailler J.-P., Richter H.T., Rosengarth A.,
RA Needleman R., Lanyi J.K.;
RT "Coupling photoisomerization of retinal to directional transport in
RT bacteriorhodopsin.";
RL J. Mol. Biol. 300:1237-1255(2000).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-245 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, AND TOPOLOGY.
RX PubMed=10949307; DOI=10.1038/35020599;
RA Royant A., Edman K., Ursby T., Pebay-Peyroula E., Landau E.M., Neutze R.;
RT "Helix deformation is coupled to vectorial proton transport in the
RT photocycle of bacteriorhodopsin.";
RL Nature 406:645-648(2000).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, FUNCTION, AND TOPOLOGY.
RX PubMed=10949309; DOI=10.1038/35020614;
RA Subramaniam S., Henderson R.;
RT "Molecular mechanism of vectorial proton translocation by
RT bacteriorhodopsin.";
RL Nature 406:653-657(2000).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 14-244 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, AND TOPOLOGY.
RX PubMed=11829498; DOI=10.1006/jmbi.2001.5295;
RA Faham S., Bowie J.U.;
RT "Bicelle crystallization: a new method for crystallizing membrane proteins
RT yields a monomeric bacteriorhodopsin structure.";
RL J. Mol. Biol. 316:1-6(2002).
RN [27] {ECO:0007744|PDB:5B6V, ECO:0007744|PDB:5B6W, ECO:0007744|PDB:5B6X, ECO:0007744|PDB:5B6Y, ECO:0007744|PDB:5B6Z, ECO:0007744|PDB:5H2H, ECO:0007744|PDB:5H2I, ECO:0007744|PDB:5H2J, ECO:0007744|PDB:5H2K, ECO:0007744|PDB:5H2L}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 14-261 IN COMPLEX WITH
RP ALL-TRANS-RETINAL, TOPOLOGY, AND FUNCTION.
RX PubMed=28008064; DOI=10.1126/science.aah3497;
RA Nango E., Royant A., Kubo M., Nakane T., Wickstrand C., Kimura T.,
RA Tanaka T., Tono K., Song C., Tanaka R., Arima T., Yamashita A.,
RA Kobayashi J., Hosaka T., Mizohata E., Nogly P., Sugahara M., Nam D.,
RA Nomura T., Shimamura T., Im D., Fujiwara T., Yamanaka Y., Jeon B.,
RA Nishizawa T., Oda K., Fukuda M., Andersson R., Bath P., Dods R.,
RA Davidsson J., Matsuoka S., Kawatake S., Murata M., Nureki O., Owada S.,
RA Kameshima T., Hatsui T., Joti Y., Schertler G., Yabashi M., Bondar A.N.,
RA Standfuss J., Neutze R., Iwata S.;
RT "A three-dimensional movie of structural changes in bacteriorhodopsin.";
RL Science 354:1552-1557(2016).
CC -!- FUNCTION: Light-driven proton pump. {ECO:0000305|PubMed:10903866,
CC ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10452895,
CC ECO:0000269|PubMed:2614846, ECO:0000269|PubMed:9287223,
CC ECO:0000269|PubMed:9632391, ECO:0000269|PubMed:9751724}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:6706999};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10452895,
CC ECO:0000269|PubMed:10467143, ECO:0000269|PubMed:10548112,
CC ECO:0000269|PubMed:10903866, ECO:0000269|PubMed:10949309,
CC ECO:0000269|PubMed:11829498, ECO:0000269|PubMed:2614846,
CC ECO:0000269|PubMed:28008064, ECO:0000269|PubMed:6706999,
CC ECO:0000269|PubMed:9287223, ECO:0000269|PubMed:9632391,
CC ECO:0000269|PubMed:9751724}.
CC -!- PTM: The covalent binding of retinal to the apoprotein, bacterioopsin,
CC generates bacteriorhodopsin. {ECO:0000269|PubMed:10452895,
CC ECO:0000269|PubMed:10467143, ECO:0000269|PubMed:10548112,
CC ECO:0000269|PubMed:10903866, ECO:0000269|PubMed:10949307,
CC ECO:0000269|PubMed:10949309, ECO:0000269|PubMed:11829498,
CC ECO:0000269|PubMed:28008064, ECO:0000269|PubMed:6706999,
CC ECO:0000269|PubMed:6794028, ECO:0000269|PubMed:9287223,
CC ECO:0000269|PubMed:9632391, ECO:0000269|PubMed:9751724}.
CC -!- MASS SPECTROMETRY: Mass=27052.5; Mass_error=2.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9655347};
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; V00474; CAA23744.1; -; Genomic_DNA.
DR EMBL; M11720; AAA72504.1; -; Genomic_DNA.
DR EMBL; X70293; CAA49774.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19772.1; -; Genomic_DNA.
DR PIR; A93898; RAHSB.
DR PIR; H84300; H84300.
DR PDB; 1AP9; X-ray; 2.35 A; A=14-261.
DR PDB; 1AT9; X-ray; 3.00 A; A=15-261.
DR PDB; 1BCT; NMR; -; A=176-244.
DR PDB; 1BHA; NMR; -; A=14-84.
DR PDB; 1BHB; NMR; -; A=14-84.
DR PDB; 1BM1; X-ray; 3.50 A; A=15-261.
DR PDB; 1BRD; EM; -; A=15-261.
DR PDB; 1BRR; X-ray; 2.90 A; A/B/C=15-261.
DR PDB; 1BRX; X-ray; 2.30 A; A=15-261.
DR PDB; 1C3W; X-ray; 1.55 A; A=18-244.
DR PDB; 1C8R; X-ray; 1.80 A; A=14-262.
DR PDB; 1C8S; X-ray; 2.00 A; A=18-235.
DR PDB; 1CWQ; X-ray; 2.25 A; A/B=14-261.
DR PDB; 1DZE; X-ray; 2.50 A; A=14-261.
DR PDB; 1E0P; X-ray; 2.10 A; A=18-245.
DR PDB; 1F4Z; X-ray; 1.80 A; A=18-244.
DR PDB; 1F50; X-ray; 1.70 A; A=18-244.
DR PDB; 1FBB; X-ray; 3.20 A; A=14-261.
DR PDB; 1FBK; X-ray; 3.20 A; A=14-261.
DR PDB; 1IW6; X-ray; 2.30 A; A=14-261.
DR PDB; 1IW9; X-ray; 2.50 A; A=14-261.
DR PDB; 1IXF; X-ray; 2.60 A; A=14-261.
DR PDB; 1JV6; X-ray; 2.00 A; A=14-262.
DR PDB; 1JV7; X-ray; 2.25 A; A=14-262.
DR PDB; 1KG8; X-ray; 2.00 A; A=14-244.
DR PDB; 1KG9; X-ray; 1.81 A; A=14-244.
DR PDB; 1KGB; X-ray; 1.65 A; A=14-244.
DR PDB; 1KME; X-ray; 2.00 A; A/B=14-244.
DR PDB; 1L0M; NMR; -; A=20-231.
DR PDB; 1M0K; X-ray; 1.43 A; A=1-262.
DR PDB; 1M0L; X-ray; 1.47 A; A=1-262.
DR PDB; 1M0M; X-ray; 1.43 A; A=1-262.
DR PDB; 1MGY; X-ray; 2.00 A; A=14-262.
DR PDB; 1O0A; X-ray; 1.62 A; A=14-262.
DR PDB; 1P8H; X-ray; 1.52 A; A=14-262.
DR PDB; 1P8I; X-ray; 1.86 A; A=14-262.
DR PDB; 1P8U; X-ray; 1.62 A; A=14-262.
DR PDB; 1PXR; X-ray; 1.70 A; A/B=14-262.
DR PDB; 1PXS; X-ray; 2.20 A; A/B=14-262.
DR PDB; 1PY6; X-ray; 1.80 A; A/B=14-262.
DR PDB; 1Q5I; X-ray; 2.30 A; A/B=14-262.
DR PDB; 1Q5J; X-ray; 2.10 A; A/B=14-262.
DR PDB; 1QHJ; X-ray; 1.90 A; A=14-261.
DR PDB; 1QKO; X-ray; 2.10 A; A=14-261.
DR PDB; 1QKP; X-ray; 2.10 A; A=14-261.
DR PDB; 1QM8; X-ray; 2.50 A; A=14-261.
DR PDB; 1R2N; NMR; -; A=14-262.
DR PDB; 1R84; NMR; -; A=14-245.
DR PDB; 1S51; X-ray; 2.00 A; A/B=18-244.
DR PDB; 1S52; X-ray; 2.30 A; A/B=18-244.
DR PDB; 1S53; X-ray; 2.00 A; A/B=18-244.
DR PDB; 1S54; X-ray; 2.20 A; A/B=18-244.
DR PDB; 1S8J; X-ray; 2.30 A; A=14-262.
DR PDB; 1S8L; X-ray; 2.30 A; A=14-262.
DR PDB; 1TN0; X-ray; 2.50 A; A/B=14-262.
DR PDB; 1TN5; X-ray; 2.20 A; A/B=14-262.
DR PDB; 1UCQ; X-ray; 2.40 A; A=14-262.
DR PDB; 1VJM; X-ray; 2.30 A; A=14-262.
DR PDB; 1X0I; X-ray; 2.30 A; 1=14-261.
DR PDB; 1X0K; X-ray; 2.60 A; 1=14-261.
DR PDB; 1X0S; X-ray; 2.50 A; A=14-261.
DR PDB; 1XJI; X-ray; 2.20 A; A=15-261.
DR PDB; 2AT9; EM; 3.00 A; A=15-261.
DR PDB; 2BRD; X-ray; 3.50 A; A=15-261.
DR PDB; 2I1X; X-ray; 2.00 A; A=14-262.
DR PDB; 2I20; X-ray; 2.08 A; A=14-262.
DR PDB; 2I21; X-ray; 1.84 A; A=14-262.
DR PDB; 2NTU; X-ray; 1.53 A; A=14-262.
DR PDB; 2NTW; X-ray; 1.53 A; A=14-262.
DR PDB; 2WJK; X-ray; 2.30 A; A=14-262.
DR PDB; 2WJL; X-ray; 2.15 A; A=14-262.
DR PDB; 2ZFE; X-ray; 2.50 A; A=1-262.
DR PDB; 2ZZL; X-ray; 2.03 A; A=1-262.
DR PDB; 3COC; X-ray; 2.31 A; A/B=14-262.
DR PDB; 3COD; X-ray; 2.70 A; A/B=14-262.
DR PDB; 3HAN; X-ray; 2.75 A; A=14-262.
DR PDB; 3HAO; X-ray; 2.49 A; A/B=14-262.
DR PDB; 3HAP; X-ray; 1.60 A; A=14-262.
DR PDB; 3HAQ; X-ray; 2.30 A; A=14-262.
DR PDB; 3HAR; X-ray; 1.70 A; A=14-262.
DR PDB; 3HAS; X-ray; 1.90 A; A=14-262.
DR PDB; 3MBV; X-ray; 2.00 A; A=14-261.
DR PDB; 3NS0; X-ray; 1.78 A; A=14-261.
DR PDB; 3NSB; X-ray; 1.78 A; A=14-261.
DR PDB; 3T45; X-ray; 3.01 A; A/B/C=20-244.
DR PDB; 3UTV; X-ray; 2.06 A; A=14-262.
DR PDB; 3UTW; X-ray; 2.40 A; A=14-262.
DR PDB; 3UTX; X-ray; 2.47 A; A/B=14-262.
DR PDB; 3UTY; X-ray; 2.37 A; A/B=14-262.
DR PDB; 3VHZ; X-ray; 2.30 A; A=1-262.
DR PDB; 3VI0; X-ray; 2.30 A; A=1-262.
DR PDB; 4FPD; X-ray; 2.65 A; A=1-262.
DR PDB; 4HWL; X-ray; 2.00 A; A/B=1-262.
DR PDB; 4HYX; X-ray; 1.99 A; A/B=1-262.
DR PDB; 4MD1; X-ray; 1.73 A; A=14-261.
DR PDB; 4MD2; X-ray; 1.73 A; A=14-261.
DR PDB; 4OV0; X-ray; 2.00 A; A=14-262.
DR PDB; 4X31; X-ray; 2.40 A; A=18-246.
DR PDB; 4X32; X-ray; 1.90 A; A=18-245.
DR PDB; 4XXJ; X-ray; 1.90 A; A/B/C=14-262.
DR PDB; 5A44; X-ray; 2.29 A; A=14-261.
DR PDB; 5A45; X-ray; 2.57 A; A=14-261.
DR PDB; 5B34; X-ray; 2.10 A; A=14-262.
DR PDB; 5B35; X-ray; 2.35 A; A=14-262.
DR PDB; 5B6V; X-ray; 2.00 A; A=14-261.
DR PDB; 5B6W; X-ray; 2.10 A; A=14-261.
DR PDB; 5B6X; X-ray; 2.10 A; A=14-261.
DR PDB; 5B6Y; X-ray; 2.10 A; A=14-261.
DR PDB; 5B6Z; X-ray; 2.10 A; A=14-261.
DR PDB; 5BR2; X-ray; 1.80 A; A=14-262.
DR PDB; 5BR5; X-ray; 2.00 A; A=14-262.
DR PDB; 5H2H; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2I; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2J; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2K; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2L; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2M; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2N; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2O; X-ray; 2.10 A; A=14-261.
DR PDB; 5H2P; X-ray; 2.10 A; A=14-261.
DR PDB; 5J7A; X-ray; 2.30 A; A=18-244.
DR PDB; 5VN7; X-ray; 2.70 A; A/B=1-262.
DR PDB; 5VN9; X-ray; 2.59 A; A/B=1-262.
DR PDB; 5ZIL; X-ray; 1.29 A; A=18-246.
DR PDB; 5ZIM; X-ray; 1.25 A; A=18-245.
DR PDB; 5ZIN; X-ray; 1.27 A; A=18-245.
DR PDB; 6G7H; X-ray; 1.50 A; A=14-261.
DR PDB; 6G7I; X-ray; 1.90 A; A=1-262.
DR PDB; 6G7J; X-ray; 1.90 A; A=1-262.
DR PDB; 6G7K; X-ray; 1.90 A; A=1-262.
DR PDB; 6G7L; X-ray; 1.90 A; A=1-262.
DR PDB; 6GA1; X-ray; 1.70 A; A=14-262.
DR PDB; 6GA2; X-ray; 1.80 A; A=14-262.
DR PDB; 6GA3; X-ray; 2.10 A; A=14-262.
DR PDB; 6GA4; X-ray; 1.80 A; A=14-262.
DR PDB; 6GA5; X-ray; 1.90 A; A=14-262.
DR PDB; 6GA6; X-ray; 1.80 A; A=14-262.
DR PDB; 6GA7; X-ray; 1.80 A; A=14-247.
DR PDB; 6GA8; X-ray; 1.80 A; A=14-262.
DR PDB; 6GA9; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAA; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAB; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAC; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAD; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAE; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAF; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAG; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAH; X-ray; 1.80 A; A=14-262.
DR PDB; 6GAI; X-ray; 1.80 A; A=14-262.
DR PDB; 6RMK; X-ray; 1.80 A; A=17-247.
DR PDB; 6RNJ; X-ray; 2.60 A; A=18-246.
DR PDB; 6RPH; X-ray; 2.60 A; A=1-240.
DR PDB; 6RQO; X-ray; 2.00 A; A=18-240.
DR PDB; 6RQP; X-ray; 1.80 A; A=18-246.
DR PDB; 7VSO; X-ray; 2.35 A; A=14-262.
DR PDBsum; 1AP9; -.
DR PDBsum; 1AT9; -.
DR PDBsum; 1BCT; -.
DR PDBsum; 1BHA; -.
DR PDBsum; 1BHB; -.
DR PDBsum; 1BM1; -.
DR PDBsum; 1BRD; -.
DR PDBsum; 1BRR; -.
DR PDBsum; 1BRX; -.
DR PDBsum; 1C3W; -.
DR PDBsum; 1C8R; -.
DR PDBsum; 1C8S; -.
DR PDBsum; 1CWQ; -.
DR PDBsum; 1DZE; -.
DR PDBsum; 1E0P; -.
DR PDBsum; 1F4Z; -.
DR PDBsum; 1F50; -.
DR PDBsum; 1FBB; -.
DR PDBsum; 1FBK; -.
DR PDBsum; 1IW6; -.
DR PDBsum; 1IW9; -.
DR PDBsum; 1IXF; -.
DR PDBsum; 1JV6; -.
DR PDBsum; 1JV7; -.
DR PDBsum; 1KG8; -.
DR PDBsum; 1KG9; -.
DR PDBsum; 1KGB; -.
DR PDBsum; 1KME; -.
DR PDBsum; 1L0M; -.
DR PDBsum; 1M0K; -.
DR PDBsum; 1M0L; -.
DR PDBsum; 1M0M; -.
DR PDBsum; 1MGY; -.
DR PDBsum; 1O0A; -.
DR PDBsum; 1P8H; -.
DR PDBsum; 1P8I; -.
DR PDBsum; 1P8U; -.
DR PDBsum; 1PXR; -.
DR PDBsum; 1PXS; -.
DR PDBsum; 1PY6; -.
DR PDBsum; 1Q5I; -.
DR PDBsum; 1Q5J; -.
DR PDBsum; 1QHJ; -.
DR PDBsum; 1QKO; -.
DR PDBsum; 1QKP; -.
DR PDBsum; 1QM8; -.
DR PDBsum; 1R2N; -.
DR PDBsum; 1R84; -.
DR PDBsum; 1S51; -.
DR PDBsum; 1S52; -.
DR PDBsum; 1S53; -.
DR PDBsum; 1S54; -.
DR PDBsum; 1S8J; -.
DR PDBsum; 1S8L; -.
DR PDBsum; 1TN0; -.
DR PDBsum; 1TN5; -.
DR PDBsum; 1UCQ; -.
DR PDBsum; 1VJM; -.
DR PDBsum; 1X0I; -.
DR PDBsum; 1X0K; -.
DR PDBsum; 1X0S; -.
DR PDBsum; 1XJI; -.
DR PDBsum; 2AT9; -.
DR PDBsum; 2BRD; -.
DR PDBsum; 2I1X; -.
DR PDBsum; 2I20; -.
DR PDBsum; 2I21; -.
DR PDBsum; 2NTU; -.
DR PDBsum; 2NTW; -.
DR PDBsum; 2WJK; -.
DR PDBsum; 2WJL; -.
DR PDBsum; 2ZFE; -.
DR PDBsum; 2ZZL; -.
DR PDBsum; 3COC; -.
DR PDBsum; 3COD; -.
DR PDBsum; 3HAN; -.
DR PDBsum; 3HAO; -.
DR PDBsum; 3HAP; -.
DR PDBsum; 3HAQ; -.
DR PDBsum; 3HAR; -.
DR PDBsum; 3HAS; -.
DR PDBsum; 3MBV; -.
DR PDBsum; 3NS0; -.
DR PDBsum; 3NSB; -.
DR PDBsum; 3T45; -.
DR PDBsum; 3UTV; -.
DR PDBsum; 3UTW; -.
DR PDBsum; 3UTX; -.
DR PDBsum; 3UTY; -.
DR PDBsum; 3VHZ; -.
DR PDBsum; 3VI0; -.
DR PDBsum; 4FPD; -.
DR PDBsum; 4HWL; -.
DR PDBsum; 4HYX; -.
DR PDBsum; 4MD1; -.
DR PDBsum; 4MD2; -.
DR PDBsum; 4OV0; -.
DR PDBsum; 4X31; -.
DR PDBsum; 4X32; -.
DR PDBsum; 4XXJ; -.
DR PDBsum; 5A44; -.
DR PDBsum; 5A45; -.
DR PDBsum; 5B34; -.
DR PDBsum; 5B35; -.
DR PDBsum; 5B6V; -.
DR PDBsum; 5B6W; -.
DR PDBsum; 5B6X; -.
DR PDBsum; 5B6Y; -.
DR PDBsum; 5B6Z; -.
DR PDBsum; 5BR2; -.
DR PDBsum; 5BR5; -.
DR PDBsum; 5H2H; -.
DR PDBsum; 5H2I; -.
DR PDBsum; 5H2J; -.
DR PDBsum; 5H2K; -.
DR PDBsum; 5H2L; -.
DR PDBsum; 5H2M; -.
DR PDBsum; 5H2N; -.
DR PDBsum; 5H2O; -.
DR PDBsum; 5H2P; -.
DR PDBsum; 5J7A; -.
DR PDBsum; 5VN7; -.
DR PDBsum; 5VN9; -.
DR PDBsum; 5ZIL; -.
DR PDBsum; 5ZIM; -.
DR PDBsum; 5ZIN; -.
DR PDBsum; 6G7H; -.
DR PDBsum; 6G7I; -.
DR PDBsum; 6G7J; -.
DR PDBsum; 6G7K; -.
DR PDBsum; 6G7L; -.
DR PDBsum; 6GA1; -.
DR PDBsum; 6GA2; -.
DR PDBsum; 6GA3; -.
DR PDBsum; 6GA4; -.
DR PDBsum; 6GA5; -.
DR PDBsum; 6GA6; -.
DR PDBsum; 6GA7; -.
DR PDBsum; 6GA8; -.
DR PDBsum; 6GA9; -.
DR PDBsum; 6GAA; -.
DR PDBsum; 6GAB; -.
DR PDBsum; 6GAC; -.
DR PDBsum; 6GAD; -.
DR PDBsum; 6GAE; -.
DR PDBsum; 6GAF; -.
DR PDBsum; 6GAG; -.
DR PDBsum; 6GAH; -.
DR PDBsum; 6GAI; -.
DR PDBsum; 6RMK; -.
DR PDBsum; 6RNJ; -.
DR PDBsum; 6RPH; -.
DR PDBsum; 6RQO; -.
DR PDBsum; 6RQP; -.
DR PDBsum; 7VSO; -.
DR AlphaFoldDB; P02945; -.
DR BMRB; P02945; -.
DR PCDDB; P02945; -.
DR SASBDB; P02945; -.
DR SMR; P02945; -.
DR DIP; DIP-59007N; -.
DR STRING; 64091.VNG_1467G; -.
DR TCDB; 3.E.1.1.1; the ion-translocating microbial rhodopsin (mr) family.
DR PaxDb; P02945; -.
DR EnsemblBacteria; AAG19772; AAG19772; VNG_1467G.
DR KEGG; hal:VNG_1467G; -.
DR PATRIC; fig|64091.14.peg.1122; -.
DR HOGENOM; CLU_054785_5_1_2; -.
DR InParanoid; P02945; -.
DR OMA; VGWAIYP; -.
DR PhylomeDB; P02945; -.
DR EvolutionaryTrace; P02945; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR InterPro; IPR001425; Arc/bac/fun_rhodopsins.
DR InterPro; IPR018229; Rhodopsin_retinal_BS.
DR PANTHER; PTHR28286; PTHR28286; 1.
DR Pfam; PF01036; Bac_rhodopsin; 1.
DR PRINTS; PR00251; BACTRLOPSIN.
DR SMART; SM01021; Bac_rhodopsin; 1.
DR PROSITE; PS00950; BACTERIAL_OPSIN_1; 1.
DR PROSITE; PS00327; BACTERIAL_OPSIN_RET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chromophore; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Photoreceptor protein;
KW Pyrrolidone carboxylic acid; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..13
FT /evidence="ECO:0000269|PubMed:291920,
FT ECO:0000269|PubMed:9541408, ECO:0000269|Ref.6"
FT /id="PRO_0000020246"
FT CHAIN 14..262
FT /note="Bacteriorhodopsin"
FT /evidence="ECO:0000269|PubMed:291920, ECO:0000269|Ref.6"
FT /id="PRO_0000020247"
FT TOPO_DOM 14..22
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TRANSMEM 23..42
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TOPO_DOM 43..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TRANSMEM 57..75
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TOPO_DOM 76..92
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TRANSMEM 93..109
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TOPO_DOM 110..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TRANSMEM 121..140
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TOPO_DOM 141..147
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TRANSMEM 148..167
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TOPO_DOM 168..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TRANSMEM 186..204
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TOPO_DOM 205..216
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TRANSMEM 217..236
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT TOPO_DOM 237..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W"
FT SITE 98
FT /note="Primary proton acceptor"
FT /evidence="ECO:0000305|PubMed:10903866,
FT ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064"
FT MOD_RES 14
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9541408"
FT MOD_RES 229
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000269|PubMed:10452895,
FT ECO:0000269|PubMed:10467143, ECO:0000269|PubMed:10548112,
FT ECO:0000269|PubMed:10903866, ECO:0000269|PubMed:10949307,
FT ECO:0000269|PubMed:10949309, ECO:0000269|PubMed:11829498,
FT ECO:0000269|PubMed:28008064, ECO:0000269|PubMed:6794028,
FT ECO:0000269|PubMed:9287223, ECO:0000269|PubMed:9632391,
FT ECO:0000269|PubMed:9751724, ECO:0007744|PDB:1C3W,
FT ECO:0007744|PDB:1F50, ECO:0007744|PDB:1IW9,
FT ECO:0007744|PDB:1KG8, ECO:0007744|PDB:1KG9,
FT ECO:0007744|PDB:1M0L, ECO:0007744|PDB:1M0M,
FT ECO:0007744|PDB:1O0A, ECO:0007744|PDB:1P8H,
FT ECO:0007744|PDB:1P8U, ECO:0007744|PDB:1Q5J,
FT ECO:0007744|PDB:1QHJ, ECO:0007744|PDB:1QKP,
FT ECO:0007744|PDB:1QM8, ECO:0007744|PDB:1R2N,
FT ECO:0007744|PDB:1R84, ECO:0007744|PDB:1S8J,
FT ECO:0007744|PDB:1TN0, ECO:0007744|PDB:1TN5,
FT ECO:0007744|PDB:1UCQ, ECO:0007744|PDB:1X0I,
FT ECO:0007744|PDB:1X0K, ECO:0007744|PDB:1X0S,
FT ECO:0007744|PDB:1XJI, ECO:0007744|PDB:2AT9,
FT ECO:0007744|PDB:2BRD, ECO:0007744|PDB:2I1X,
FT ECO:0007744|PDB:2I20, ECO:0007744|PDB:2I21,
FT ECO:0007744|PDB:2NTU, ECO:0007744|PDB:2NTW,
FT ECO:0007744|PDB:2WJK, ECO:0007744|PDB:2WJL,
FT ECO:0007744|PDB:2ZFE, ECO:0007744|PDB:2ZZL,
FT ECO:0007744|PDB:3COD, ECO:0007744|PDB:3HAN,
FT ECO:0007744|PDB:3HAO, ECO:0007744|PDB:3HAP,
FT ECO:0007744|PDB:3HAQ, ECO:0007744|PDB:3HAR,
FT ECO:0007744|PDB:3HAS, ECO:0007744|PDB:3NS0,
FT ECO:0007744|PDB:3NSB, ECO:0007744|PDB:3T45,
FT ECO:0007744|PDB:3UTV, ECO:0007744|PDB:3UTW,
FT ECO:0007744|PDB:3UTX, ECO:0007744|PDB:3VHZ,
FT ECO:0007744|PDB:3VI0, ECO:0007744|PDB:4FPD,
FT ECO:0007744|PDB:4HWL, ECO:0007744|PDB:4MD1,
FT ECO:0007744|PDB:4MD2, ECO:0007744|PDB:4X31,
FT ECO:0007744|PDB:4X32, ECO:0007744|PDB:5A44,
FT ECO:0007744|PDB:5A45, ECO:0007744|PDB:5B34,
FT ECO:0007744|PDB:5B6V, ECO:0007744|PDB:5B6W,
FT ECO:0007744|PDB:5B6X, ECO:0007744|PDB:5B6Y,
FT ECO:0007744|PDB:5B6Z, ECO:0007744|PDB:5BR2,
FT ECO:0007744|PDB:5BR5, ECO:0007744|PDB:5H2H,
FT ECO:0007744|PDB:5H2I, ECO:0007744|PDB:5H2J,
FT ECO:0007744|PDB:5H2K, ECO:0007744|PDB:5H2L,
FT ECO:0007744|PDB:5H2M, ECO:0007744|PDB:5H2N,
FT ECO:0007744|PDB:5H2O, ECO:0007744|PDB:5H2P,
FT ECO:0007744|PDB:5J7A"
FT CONFLICT 118
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="L -> I (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="I -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="Missing (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="L -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="L -> A (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:1QKO"
FT HELIX 23..44
FT /evidence="ECO:0007829|PDB:5ZIM"
FT HELIX 50..74
FT /evidence="ECO:0007829|PDB:5ZIM"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:5ZIM"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5ZIM"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5ZIM"
FT HELIX 94..113
FT /evidence="ECO:0007829|PDB:5ZIM"
FT HELIX 118..140
FT /evidence="ECO:0007829|PDB:5ZIM"
FT HELIX 144..167
FT /evidence="ECO:0007829|PDB:5ZIM"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4X31"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:5ZIM"
FT HELIX 178..204
FT /evidence="ECO:0007829|PDB:5ZIM"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:5ZIM"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4FPD"
FT HELIX 214..237
FT /evidence="ECO:0007829|PDB:5ZIM"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5ZIM"
SQ SEQUENCE 262 AA; 28256 MW; 38AC8A364C8C7F21 CRC64;
MLELLPTAVE GVSQAQITGR PEWIWLALGT ALMGLGTLYF LVKGMGVSDP DAKKFYAITT
LVPAIAFTMY LSMLLGYGLT MVPFGGEQNP IYWARYADWL FTTPLLLLDL ALLVDADQGT
ILALVGADGI MIGTGLVGAL TKVYSYRFVW WAISTAAMLY ILYVLFFGFT SKAESMRPEV
ASTFKVLRNV TVVLWSAYPV VWLIGSEGAG IVPLNIETLL FMVLDVSAKV GFGLILLRSR
AIFGEAEAPE PSAGDGAAAT SD
