PSBC_THEVB
ID PSBC_THEVB Reviewed; 461 AA.
AC Q8DIF8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE AltName: Full=PSII 43 kDa protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE AltName: Full=Protein CP-43 {ECO:0000255|HAMAP-Rule:MF_01496};
GN Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496}; OrderedLocusNames=tlr1631;
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 [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 [2]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 2-461 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 [3]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH
RP MANGANESE, COFACTOR, 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 [4]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH
RP MANGANESE, 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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE,
RP COFACTOR, 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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE,
RP FUNCTION, 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 [7]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE,
RP FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE,
RP COFACTOR, 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 [9]
RP X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE,
RP COFACTOR, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 7-461 IN PHOTOSYSTEM II WITH
RP MANGANESE, 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 [11]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE,
RP FUNCTION, 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_01496,
CC ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:25006873}.
CC -!- COFACTOR:
CC Note=Binds multiple chlorophylls and provides some of the ligands for
CC the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also
CC provide a ligand for a Cl- that is required for oxygen evolution. PSII
CC binds additional chlorophylls, carotenoids and specific lipids.
CC {ECO:0000255|HAMAP-Rule:MF_01496, 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.2};
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_01496,
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.2}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01496, 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.2}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01496, 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.2}.
CC -!- MASS SPECTROMETRY: Mass=51704; Mass_error=87; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19219048};
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
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DR EMBL; BA000039; BAC09183.2; -; Genomic_DNA.
DR RefSeq; NP_682421.1; NC_004113.1.
DR RefSeq; WP_024124637.1; NC_004113.1.
DR PDB; 1S5L; X-ray; 3.50 A; C/c=2-461.
DR PDB; 1W5C; X-ray; 3.20 A; C/I=2-461.
DR PDB; 2AXT; X-ray; 3.00 A; C/c=2-461.
DR PDB; 3KZI; X-ray; 3.60 A; C=1-461.
DR PDB; 4FBY; X-ray; 6.56 A; C/P=1-461.
DR PDB; 4IXQ; X-ray; 5.70 A; C/c=1-461.
DR PDB; 4IXR; X-ray; 5.90 A; C/c=1-461.
DR PDB; 4PBU; X-ray; 5.00 A; C/c=7-461.
DR PDB; 4PJ0; X-ray; 2.44 A; C/c=1-461.
DR PDB; 4RVY; X-ray; 5.50 A; C/c=1-461.
DR PDB; 4TNH; X-ray; 4.90 A; C/c=1-461.
DR PDB; 4TNI; X-ray; 4.60 A; C/c=1-461.
DR PDB; 4TNJ; X-ray; 4.50 A; C/c=1-461.
DR PDB; 4TNK; X-ray; 5.20 A; C/c=1-461.
DR PDB; 4V62; X-ray; 2.90 A; AC/BC=1-461.
DR PDB; 4V82; X-ray; 3.20 A; AC/BC=1-461.
DR PDB; 5E79; X-ray; 3.50 A; C/c=11-461.
DR PDB; 5E7C; X-ray; 4.50 A; C/c=11-461.
DR PDB; 5H2F; X-ray; 2.20 A; C/c=7-461.
DR PDB; 5KAF; X-ray; 3.00 A; C/c=1-461.
DR PDB; 5KAI; X-ray; 2.80 A; C/c=1-461.
DR PDB; 5MX2; X-ray; 2.20 A; C/c=1-461.
DR PDB; 5TIS; X-ray; 2.25 A; C/c=1-461.
DR PDB; 5ZZN; X-ray; 2.10 A; C/c=7-461.
DR PDB; 6DHE; X-ray; 2.05 A; C/c=11-461.
DR PDB; 6DHF; X-ray; 2.08 A; C/c=11-461.
DR PDB; 6DHG; X-ray; 2.50 A; C/c=11-461.
DR PDB; 6DHH; X-ray; 2.20 A; C/c=11-461.
DR PDB; 6DHO; X-ray; 2.07 A; C/c=11-461.
DR PDB; 6DHP; X-ray; 2.04 A; C/c=11-461.
DR PDB; 6W1O; X-ray; 2.08 A; C/c=1-461.
DR PDB; 6W1P; X-ray; 2.26 A; C/c=1-461.
DR PDB; 6W1Q; X-ray; 2.27 A; C/c=1-461.
DR PDB; 6W1R; X-ray; 2.23 A; C/c=1-461.
DR PDB; 6W1T; X-ray; 2.01 A; C/c=1-461.
DR PDB; 6W1U; X-ray; 2.09 A; C/c=1-461.
DR PDB; 6W1V; X-ray; 2.09 A; C/c=1-461.
DR PDB; 7NHO; EM; 2.66 A; C=1-461.
DR PDB; 7NHP; EM; 2.72 A; C=1-461.
DR PDB; 7NHQ; EM; 2.68 A; C=1-461.
DR PDB; 7RF1; X-ray; 1.89 A; C/c=1-461.
DR PDB; 7RF2; X-ray; 2.08 A; C/c=1-461.
DR PDB; 7RF3; X-ray; 2.26 A; C/c=1-461.
DR PDB; 7RF4; X-ray; 2.27 A; C/c=1-461.
DR PDB; 7RF5; X-ray; 2.23 A; C/c=1-461.
DR PDB; 7RF6; X-ray; 2.01 A; C/c=1-461.
DR PDB; 7RF7; X-ray; 2.09 A; C/c=1-461.
DR PDB; 7RF8; X-ray; 2.09 A; C/c=1-461.
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; Q8DIF8; -.
DR SMR; Q8DIF8; -.
DR DIP; DIP-48489N; -.
DR IntAct; Q8DIF8; 1.
DR STRING; 197221.163937831; -.
DR EnsemblBacteria; BAC09183; BAC09183; BAC09183.
DR KEGG; tel:tlr1631; -.
DR PATRIC; fig|197221.4.peg.1711; -.
DR eggNOG; ENOG502Z7VA; Bacteria.
DR OMA; WKDKNKM; -.
DR OrthoDB; 166907at2; -.
DR EvolutionaryTrace; Q8DIF8; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR Gene3D; 1.10.10.670; -; 1.
DR HAMAP; MF_01496; PSII_PsbC_CP43; 1.
DR InterPro; IPR000932; PS_antenna-like.
DR InterPro; IPR036001; PS_II_antenna-like_sf.
DR InterPro; IPR005869; PSII_PsbC.
DR InterPro; IPR044900; PSII_PsbC_sf.
DR PANTHER; PTHR33180; PTHR33180; 1.
DR Pfam; PF00421; PSII; 1.
DR SUPFAM; SSF161077; SSF161077; 1.
DR TIGRFAMs; TIGR01153; psbC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll; Chromophore; Manganese; Membrane; Metal-binding;
KW Photosynthesis; Photosystem II; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..461
FT /note="Photosystem II CP43 reaction center protein"
FT /id="PRO_0000430807"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 39..53
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 54..104
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 105..118
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 119..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 148..161
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 162..226
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 227..240
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 241..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 260..273
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 274..417
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 418..432
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 433..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT BINDING 355
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
FT ECO:0000303|PubMed:25043005"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 34..62
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:7NHP"
FT HELIX 97..122
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 142..169
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:5TIS"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 218..241
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 256..280
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 294..311
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:2AXT"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:7NHO"
FT HELIX 410..441
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:5MX2"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:5ZZN"
SQ SEQUENCE 461 AA; 50245 MW; 6A07B683DCB519B7 CRC64;
MVTLSSNSIF ATNRDQESSG FAWWAGNARL INLSGKLLGA HVAHAGLIVF WAGAMTLFEL
AHFIPEKPMY EQGLILIPHI ATLGWGVGPG GEVVDTFPFF VVGVVHLISS AVLGFGGVYH
AIRGPETLEE YSSFFGYDWK DKNKMTTILG FHLIVLGIGA LLLVAKAMFF GGLYDTWAPG
GGDVRVITNP TLDPRVIFGY LLKSPFGGEG WIVSVNNLED VVGGHIWIGL ICIAGGIWHI
LTTPFGWARR AFIWSGEAYL SYSLGALSMM GFIATCFVWF NNTVYPSEFY GPTGPEASQA
QAMTFLIRDQ KLGANVGSAQ GPTGLGKYLM RSPTGEIIFG GETMRFWDFR GPWLEPLRGP
NGLDLNKIKN DIQPWQERRA AEYMTHAPLG SLNSVGGVAT EINSVNFVSP RSWLATSHFV
LAFFFLVGHL WHAGRARAAA AGFEKGIDRE SEPVLSMPSL D
