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Database: UniProt
Entry: Q8DIF8
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Original site: Q8DIF8 
ID   PSBC_THEEB              Reviewed;         461 AA.
AC   Q8DIF8;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   02-DEC-2020, entry version 117.
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 elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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=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=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=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=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=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=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=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   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   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:0042651; C: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   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
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   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   METAL           355
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2"
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   METAL           355
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3"
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:0000244|PDB:5ZZN"
FT   HELIX           23..30
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           34..62
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           69..71
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           76..82
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          85..87
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           89..91
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           97..122
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            129..131
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            133..135
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           142..169
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          173..175
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            179..181
FT                   /evidence="ECO:0000244|PDB:5TIS"
FT   STRAND          183..185
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           194..197
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           199..202
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            207..209
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           211..214
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           218..241
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           246..251
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           256..280
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            283..286
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           287..290
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           294..311
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            316..318
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          324..331
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          337..339
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           341..346
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            352..354
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           355..357
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          360..363
FT                   /evidence="ECO:0000244|PDB:2AXT"
FT   HELIX           365..370
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           374..384
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          395..398
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           410..441
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           449..451
FT                   /evidence="ECO:0000244|PDB:5MX2"
FT   HELIX           453..456
FT                   /evidence="ECO:0000244|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
//
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