PSBB_THEVB
ID PSBB_THEVB Reviewed; 510 AA.
AC Q8DIQ1; Q9F1M3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Photosystem II CP47 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE AltName: Full=PSII 47 kDa protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE AltName: Full=Protein CP-47 {ECO:0000255|HAMAP-Rule:MF_01495};
GN Name=psbB {ECO:0000255|HAMAP-Rule:MF_01495}; OrderedLocusNames=tlr1530;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=15653799; DOI=10.1093/pcp/pch207;
RA Iwai M., Katoh H., Katayama M., Ikeuchi M.;
RT "PSII-Tc protein plays an important role in dimerization of photosystem
RT II.";
RL Plant Cell Physiol. 45:1809-1816(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-510 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX DOI=10.1039/B406989G;
RA Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.;
RT "Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a
RT closer look at the Mn-cluster.";
RL Phys. Chem. Chem. Phys. 6:4733-4736(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14764885; DOI=10.1126/science.1093087;
RA Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT "Architecture of the photosynthetic oxygen-evolving center.";
RL Science 303:1831-1838(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=16355230; DOI=10.1038/nature04224;
RA Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT photosystem II.";
RL Nature 438:1040-1044(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=19219048; DOI=10.1038/nsmb.1559;
RA Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT quinones, lipids, channels and chloride.";
RL Nat. Struct. Mol. Biol. 16:334-342(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA Zouni A.;
RT "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT elongatus at 3.6 A resolution.";
RL J. Biol. Chem. 285:26255-26262(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA Muh F., Dau H., Saenger W., Zouni A.;
RT "Structural basis of cyanobacterial photosystem II inhibition by the
RT herbicide terbutryn.";
RL J. Biol. Chem. 286:15964-15972(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA Bergmann U., Yano J., Yachandra V.K.;
RT "Room temperature femtosecond X-ray diffraction of photosystem II
RT microcrystals.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=23413188; DOI=10.1126/science.1234273;
RA Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA Yachandra V.K., Bergmann U., Yano J.;
RT "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT II at room temperature.";
RL Science 340:491-495(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 2-505 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25043005; DOI=10.1038/nature13453;
RA Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA Chapman H.N., Spence J.C., Fromme P.;
RT "Serial time-resolved crystallography of photosystem II using a femtosecond
RT X-ray laser.";
RL Nature 513:261-265(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25006873; DOI=10.1038/ncomms5371;
RA Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA Bergmann U., Yano J., Yachandra V.K.;
RT "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT diffraction and spectroscopy.";
RL Nat. Commun. 5:4371-4371(2014).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII). It binds chlorophyll and helps catalyze the primary light-
CC induced photochemical processes of PSII. PSII is a light-driven
CC water:plastoquinone oxidoreductase, using light energy to abstract
CC electrons from H(2)O, generating O(2) and a proton gradient
CC subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_01495,
CC ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:25006873}.
CC -!- COFACTOR:
CC Note=Binds multiple chlorophylls. PSII binds additional chlorophylls,
CC carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01495,
CC ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3};
CC -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01495,
CC ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01495, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
CC ECO:0000269|Ref.3}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01495, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
CC ECO:0000269|Ref.3}.
CC -!- MASS SPECTROMETRY: Mass=56485; Mass_error=108; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19219048};
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01495, ECO:0000305}.
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DR EMBL; AB052566; BAB19261.1; -; Genomic_DNA.
DR EMBL; BA000039; BAC09082.1; -; Genomic_DNA.
DR RefSeq; NP_682320.1; NC_004113.1.
DR RefSeq; WP_011057370.1; NC_004113.1.
DR PDB; 1S5L; X-ray; 3.50 A; B/b=1-510.
DR PDB; 1W5C; X-ray; 3.20 A; B/H=1-510.
DR PDB; 2AXT; X-ray; 3.00 A; B/b=1-510.
DR PDB; 3KZI; X-ray; 3.60 A; B=1-510.
DR PDB; 4FBY; X-ray; 6.56 A; B/N=1-510.
DR PDB; 4IXQ; X-ray; 5.70 A; B/b=1-510.
DR PDB; 4IXR; X-ray; 5.90 A; B/b=1-510.
DR PDB; 4PBU; X-ray; 5.00 A; B/b=2-505.
DR PDB; 4PJ0; X-ray; 2.44 A; B/b=1-510.
DR PDB; 4RVY; X-ray; 5.50 A; B/b=2-505.
DR PDB; 4TNH; X-ray; 4.90 A; B/b=1-510.
DR PDB; 4TNI; X-ray; 4.60 A; B/b=1-510.
DR PDB; 4TNJ; X-ray; 4.50 A; B/b=1-510.
DR PDB; 4TNK; X-ray; 5.20 A; B/b=1-510.
DR PDB; 4V62; X-ray; 2.90 A; AB/BB=1-510.
DR PDB; 4V82; X-ray; 3.20 A; AB/BB=1-510.
DR PDB; 5E79; X-ray; 3.50 A; B/b=2-505.
DR PDB; 5E7C; X-ray; 4.50 A; B/b=2-505.
DR PDB; 5H2F; X-ray; 2.20 A; B/b=2-506.
DR PDB; 5KAF; X-ray; 3.00 A; B/b=1-510.
DR PDB; 5KAI; X-ray; 2.80 A; B/b=1-510.
DR PDB; 5MX2; X-ray; 2.20 A; B/b=1-510.
DR PDB; 5TIS; X-ray; 2.25 A; B/b=1-510.
DR PDB; 5ZZN; X-ray; 2.10 A; B/b=2-506.
DR PDB; 6DHE; X-ray; 2.05 A; B/b=2-506.
DR PDB; 6DHF; X-ray; 2.08 A; B/b=2-506.
DR PDB; 6DHG; X-ray; 2.50 A; B/b=2-506.
DR PDB; 6DHH; X-ray; 2.20 A; B/b=2-506.
DR PDB; 6DHO; X-ray; 2.07 A; B/b=2-506.
DR PDB; 6DHP; X-ray; 2.04 A; B/b=2-506.
DR PDB; 6W1O; X-ray; 2.08 A; B/b=1-506.
DR PDB; 6W1P; X-ray; 2.26 A; B/b=1-506.
DR PDB; 6W1Q; X-ray; 2.27 A; B/b=1-506.
DR PDB; 6W1R; X-ray; 2.23 A; B/b=1-506.
DR PDB; 6W1T; X-ray; 2.01 A; B/b=1-506.
DR PDB; 6W1U; X-ray; 2.09 A; B/b=1-510.
DR PDB; 6W1V; X-ray; 2.09 A; B/b=1-510.
DR PDB; 7NHO; EM; 2.66 A; B=1-510.
DR PDB; 7NHP; EM; 2.72 A; B=1-510.
DR PDB; 7NHQ; EM; 2.68 A; B=1-510.
DR PDB; 7RF1; X-ray; 1.89 A; B/b=1-510.
DR PDB; 7RF2; X-ray; 2.08 A; B/b=1-510.
DR PDB; 7RF3; X-ray; 2.26 A; B/b=1-510.
DR PDB; 7RF4; X-ray; 2.27 A; B/b=1-510.
DR PDB; 7RF5; X-ray; 2.23 A; B/b=1-510.
DR PDB; 7RF6; X-ray; 2.01 A; B/b=1-510.
DR PDB; 7RF7; X-ray; 2.09 A; B/b=1-510.
DR PDB; 7RF8; X-ray; 2.09 A; B/b=1-510.
DR PDBsum; 1S5L; -.
DR PDBsum; 1W5C; -.
DR PDBsum; 2AXT; -.
DR PDBsum; 3KZI; -.
DR PDBsum; 4FBY; -.
DR PDBsum; 4IXQ; -.
DR PDBsum; 4IXR; -.
DR PDBsum; 4PBU; -.
DR PDBsum; 4PJ0; -.
DR PDBsum; 4RVY; -.
DR PDBsum; 4TNH; -.
DR PDBsum; 4TNI; -.
DR PDBsum; 4TNJ; -.
DR PDBsum; 4TNK; -.
DR PDBsum; 4V62; -.
DR PDBsum; 4V82; -.
DR PDBsum; 5E79; -.
DR PDBsum; 5E7C; -.
DR PDBsum; 5H2F; -.
DR PDBsum; 5KAF; -.
DR PDBsum; 5KAI; -.
DR PDBsum; 5MX2; -.
DR PDBsum; 5TIS; -.
DR PDBsum; 5ZZN; -.
DR PDBsum; 6DHE; -.
DR PDBsum; 6DHF; -.
DR PDBsum; 6DHG; -.
DR PDBsum; 6DHH; -.
DR PDBsum; 6DHO; -.
DR PDBsum; 6DHP; -.
DR PDBsum; 6W1O; -.
DR PDBsum; 6W1P; -.
DR PDBsum; 6W1Q; -.
DR PDBsum; 6W1R; -.
DR PDBsum; 6W1T; -.
DR PDBsum; 6W1U; -.
DR PDBsum; 6W1V; -.
DR PDBsum; 7NHO; -.
DR PDBsum; 7NHP; -.
DR PDBsum; 7NHQ; -.
DR PDBsum; 7RF1; -.
DR PDBsum; 7RF2; -.
DR PDBsum; 7RF3; -.
DR PDBsum; 7RF4; -.
DR PDBsum; 7RF5; -.
DR PDBsum; 7RF6; -.
DR PDBsum; 7RF7; -.
DR PDBsum; 7RF8; -.
DR AlphaFoldDB; Q8DIQ1; -.
DR SMR; Q8DIQ1; -.
DR DIP; DIP-48488N; -.
DR IntAct; Q8DIQ1; 1.
DR STRING; 197221.22295255; -.
DR EnsemblBacteria; BAC09082; BAC09082; BAC09082.
DR KEGG; tel:tlr1530; -.
DR PATRIC; fig|197221.4.peg.1607; -.
DR eggNOG; ENOG502Z7TN; Bacteria.
DR OMA; MLAAIWH; -.
DR OrthoDB; 174499at2; -.
DR EvolutionaryTrace; Q8DIQ1; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR HAMAP; MF_01495; PSII_PsbB_CP47; 1.
DR InterPro; IPR000932; PS_antenna-like.
DR InterPro; IPR036001; PS_II_antenna-like_sf.
DR InterPro; IPR017486; PSII_PsbB.
DR PANTHER; PTHR33180; PTHR33180; 1.
DR Pfam; PF00421; PSII; 1.
DR SUPFAM; SSF161077; SSF161077; 1.
DR TIGRFAMs; TIGR03039; PS_II_CP47; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll; Chromophore; Membrane; Photosynthesis;
KW Photosystem II; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19219048"
FT CHAIN 2..510
FT /note="Photosystem II CP47 reaction center protein"
FT /id="PRO_0000430806"
FT TOPO_DOM 2..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 23..37
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 38..95
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 96..109
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 110..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 142..156
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 157..200
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 201..213
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 214..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 239..252
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 253..453
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 454..468
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 469..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 16..44
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5H2F"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:7NHO"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1S5L"
FT HELIX 93..116
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7NHQ"
FT HELIX 135..155
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5TIS"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1W5C"
FT HELIX 195..218
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 234..258
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:7NHQ"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5MX2"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:7NHQ"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 336..347
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:7NHO"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:7NHO"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:7NHO"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4PJ0"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 447..474
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:7NHQ"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5ZZN"
SQ SEQUENCE 510 AA; 56604 MW; 0AEEE3DB7124FB81 CRC64;
MGLPWYRVHT VLINDPGRLI AAHLMHTALV AGWAGSMALY ELATFDPSDP VLNPMWRQGM
FVLPFMARLG VTGSWSGWSI TGETGIDPGF WSFEGVALAH IVLSGLLFLA ACWHWVYWDL
ELFRDPRTGE PALDLPKMFG IHLFLAGLLC FGFGAFHLTG LFGPGMWVSD PYGLTGSVQP
VAPEWGPDGF NPYNPGGVVA HHIAAGIVGI IAGLFHILVR PPQRLYKALR MGNIETVLSS
SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDSSYF QQEINRRVQA SLASGATLEE
AWSAIPEKLA FYDYIGNNPA KGGLFRTGPM NKGDGIAQAW KGHAVFRNKE GEELFVRRMP
AFFESFPVIL TDKNGVVKAD IPFRRAESKY SFEQQGVTVS FYGGELNGQT FTDPPTVKSY
ARKAIFGEIF EFDTETLNSD GIFRTSPRGW FTFAHAVFAL LFFFGHIWHG ARTLFRDVFS
GIDPELSPEQ VEWGFYQKVG DVTTRRKEAV
