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Database: UniProt
Entry: CY550_THEEB
LinkDB: CY550_THEEB
Original site: CY550_THEEB 
ID   CY550_THEEB             Reviewed;         163 AA.
AC   P0A386; P56150; Q9ETF4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   02-DEC-2020, entry version 117.
DE   RecName: Full=Cytochrome c-550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE   AltName: Full=Cytochrome c-549;
DE   AltName: Full=Cytochrome c550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE   AltName: Full=Low-potential cytochrome c {ECO:0000255|HAMAP-Rule:MF_01378};
DE   Flags: Precursor;
GN   Name=psbV {ECO:0000255|HAMAP-Rule:MF_01378}; OrderedLocusNames=tll1285;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX   PubMed=11427679; DOI=10.1093/pcp/pce074;
RA   Katoh H., Itoh S., Shen J.-R., Ikeuchi M.;
RT   "Functional analysis of psbV and a novel c-type cytochrome gene psbV2 of
RT   the thermophilic cyanobacterium Thermosynechococcus elongatus strain BP-
RT   1.";
RL   Plant Cell Physiol. 42:599-607(2001).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 27-33, COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
RA   Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y., Satoh K.,
RA   Sugiura M.;
RT   "Ycf12 is a core subunit in the photosystem II complex.";
RL   Biochim. Biophys. Acta 1767:1269-1275(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-163, COFACTOR, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12881497; DOI=10.1093/pcp/pcg084;
RA   Kerfeld C.A., Sawaya M.R., Bottin H., Tran K.T., Sugiura M., Cascio D.,
RA   Desbois A., Yeates T.O., Kirilovsky D., Boussac A.;
RT   "Structural and EPR characterization of the soluble form of cytochrome c-
RT   550 and of the psbV2 gene product from the cyanobacterium
RT   Thermosynechococcus elongatus.";
RL   Plant Cell Physiol. 44:697-706(2003).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP   HEME, 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   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP   HEME, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   DOI=10.1039/b406989g;
RA   Biesiadka J., Loll B., Kern J., Irrgangb 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   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP   HEME, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
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   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP   HEME, 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   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP   HEME, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP   HEME, 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   [11]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, 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   [12]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   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   [13]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP   HEME, 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   [14]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   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: Low-potential cytochrome c that plays a role in the oxygen-
CC       evolving complex of photosystem II. It is not essential for growth
CC       under normal conditions but is required under low CO(2) concentrations.
CC       PSII is a light-driven water plastoquinone oxidoreductase, using light
CC       energy to abstract electrons from H(2)O, generating a proton gradient
CC       subsequently used for ATP formation. {ECO:0000269|PubMed:11427679,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:25006873}.
CC   -!- COFACTOR:
CC       Note=Binds 1 heme group covalently per subunit. PSII binds multiple
CC       chlorophylls, carotenoids and specific lipids.
CC       {ECO:0000269|PubMed:12881497, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
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.6};
CC   -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC       PsbO, PsbP, PsbQ, PsbV and PsbU (By similarity). PsbP and PsbQ are not
CC       seen in the crystal structures; however there is biochemical evidence
CC       that they are part of the OEC. Monomer in the isolated crystal
CC       structure. 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, 3 peripheral proteins PsbO,
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12881497,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
CC       ECO:0000269|Ref.6}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01378, ECO:0000269|PubMed:12881497,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, 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.6}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01378, ECO:0000269|PubMed:12881497,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, 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.6}; Lumenal side {ECO:0000255|HAMAP-Rule:MF_01378,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, 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.6}. Note=Associated with photosystem II at the lumenal
CC       side of the thylakoid membrane.
CC   -!- MASS SPECTROMETRY: Mass=15752; Mass_error=11; Method=MALDI; Note=Mass
CC       includes covalently attached heme group.;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=15743; Method=MALDI; Note=Mass includes
CC       covalently attached heme group.;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- DISRUPTION PHENOTYPE: Cells do not grow photoautotrophically under low
CC       CO(2) concentrations. {ECO:0000269|PubMed:11427679}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01378}.
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DR   EMBL; AB052597; BAB20059.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC08837.1; -; Genomic_DNA.
DR   RefSeq; NP_682075.1; NC_004113.1.
DR   RefSeq; WP_011057125.1; NC_004113.1.
DR   PDB; 1MZ4; X-ray; 1.80 A; A=27-163.
DR   PDB; 1S5L; X-ray; 3.50 A; V/v=27-163.
DR   PDB; 1W5C; X-ray; 3.20 A; T/V=1-163.
DR   PDB; 2AXT; X-ray; 3.00 A; V/v=27-163.
DR   PDB; 3KZI; X-ray; 3.60 A; V=27-163.
DR   PDB; 4FBY; X-ray; 6.56 A; V/i=27-163.
DR   PDB; 4IXQ; X-ray; 5.70 A; V/v=1-163.
DR   PDB; 4IXR; X-ray; 5.90 A; V/v=1-163.
DR   PDB; 4PBU; X-ray; 5.00 A; V/v=27-163.
DR   PDB; 4PJ0; X-ray; 2.44 A; V/v=1-163.
DR   PDB; 4RVY; X-ray; 5.50 A; V/v=27-163.
DR   PDB; 4TNH; X-ray; 4.90 A; V/v=1-163.
DR   PDB; 4TNI; X-ray; 4.60 A; V/v=1-163.
DR   PDB; 4TNJ; X-ray; 4.50 A; V/v=1-163.
DR   PDB; 4TNK; X-ray; 5.20 A; V/v=1-163.
DR   PDB; 4V62; X-ray; 2.90 A; AV/BV=27-163.
DR   PDB; 4V82; X-ray; 3.20 A; AV/BV=27-163.
DR   PDB; 5E79; X-ray; 3.50 A; V/v=27-163.
DR   PDB; 5E7C; X-ray; 4.50 A; V/v=27-163.
DR   PDB; 5H2F; X-ray; 2.20 A; V/v=27-163.
DR   PDB; 5KAF; X-ray; 3.00 A; V/v=1-163.
DR   PDB; 5KAI; X-ray; 2.80 A; V/v=1-163.
DR   PDB; 5MX2; X-ray; 2.20 A; V/v=1-163.
DR   PDB; 5TIS; X-ray; 2.25 A; V/v=1-163.
DR   PDB; 5ZZN; X-ray; 2.10 A; V/v=27-163.
DR   PDB; 6DHE; X-ray; 2.05 A; V/v=27-163.
DR   PDB; 6DHF; X-ray; 2.08 A; V/v=27-163.
DR   PDB; 6DHG; X-ray; 2.50 A; V/v=27-163.
DR   PDB; 6DHH; X-ray; 2.20 A; V/v=27-163.
DR   PDB; 6DHO; X-ray; 2.07 A; V/v=27-163.
DR   PDB; 6DHP; X-ray; 2.04 A; V/v=27-163.
DR   PDB; 6W1O; X-ray; 2.08 A; V/v=1-163.
DR   PDB; 6W1P; X-ray; 2.26 A; V/v=1-163.
DR   PDB; 6W1Q; X-ray; 2.27 A; V/v=1-163.
DR   PDB; 6W1R; X-ray; 2.23 A; V/v=1-163.
DR   PDB; 6W1T; X-ray; 2.01 A; V/v=1-163.
DR   PDB; 6W1U; X-ray; 2.09 A; V/v=1-163.
DR   PDB; 6W1V; X-ray; 2.09 A; V/v=1-163.
DR   PDBsum; 1MZ4; -.
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; P0A386; -.
DR   DIP; DIP-48502N; -.
DR   IntAct; P0A386; 19.
DR   STRING; 197221.22295009; -.
DR   EnsemblBacteria; BAC08837; BAC08837; BAC08837.
DR   KEGG; tel:tll1285; -.
DR   PATRIC; fig|197221.4.peg.1352; -.
DR   eggNOG; COG2010; Bacteria.
DR   OMA; DYMKDPT; -.
DR   OrthoDB; 1553768at2; -.
DR   EvolutionaryTrace; P0A386; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0018063; P:cytochrome c-heme linkage; IEA:UniProtKB-UniRule.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   Gene3D; 1.10.760.10; -; 1.
DR   HAMAP; MF_01378; PSII_Cyt550; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR029490; Cytochrom_C550.
DR   InterPro; IPR016003; PSII_cyt_c550.
DR   InterPro; IPR017851; PSII_PsbV_cyt_c550.
DR   Pfam; PF14495; Cytochrom_C550; 1.
DR   PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   TIGRFAMs; TIGR03045; PS_II_C550; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Photosynthesis; Photosystem II;
KW   Reference proteome; Signal; Thylakoid; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01378,
FT                   ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048,
FT                   ECO:0000269|PubMed:20558739"
FT   CHAIN           27..163
FT                   /note="Cytochrome c-550"
FT                   /id="PRO_0000006518"
FT   METAL           67
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000269|PubMed:12881497,
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:25043005,
FT                   ECO:0000303|Ref.6"
FT   METAL           118
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000269|PubMed:12881497,
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:25043005,
FT                   ECO:0000303|Ref.6"
FT   HELIX           31..34
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   STRAND          35..39
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   STRAND          44..46
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           49..62
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           64..67
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           68..70
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   STRAND          73..75
FT                   /evidence="ECO:0000244|PDB:1W5C"
FT   HELIX           76..78
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           82..86
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   STRAND          88..90
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           95..103
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   STRAND          110..113
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   TURN            115..117
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           121..123
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   TURN            124..126
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           128..130
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           135..152
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   HELIX           153..155
FT                   /evidence="ECO:0000244|PDB:1MZ4"
FT   TURN            156..158
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           160..162
FT                   /evidence="ECO:0000244|PDB:5ZZN"
SQ   SEQUENCE   163 AA;  18027 MW;  DA634C5C4084F676 CRC64;
     MLKKCVWLAV ALCLCLWQFT MGTALAAELT PEVLTVPLNS EGKTITLTEK QYLEGKRLFQ
     YACASCHVGG ITKTNPSLDL RTETLALATP PRDNIEGLVD YMKNPTTYDG EQEIAEVHPS
     LRSADIFPKM RNLTEKDLVA IAGHILVEPK ILGDKWGGGK VYY
//
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