CY550_THEVB
ID CY550_THEVB Reviewed; 163 AA.
AC P0A386; P56150; Q9ETF4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 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], 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=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 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=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 [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=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 [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=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 [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=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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
RP HEME, 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 [14]
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: 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 Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Note=Binds 1 heme c 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 PDB; 7RF1; X-ray; 1.89 A; V/v=1-163.
DR PDB; 7RF2; X-ray; 2.08 A; V/v=1-163.
DR PDB; 7RF3; X-ray; 2.26 A; V/v=1-163.
DR PDB; 7RF4; X-ray; 2.27 A; V/v=1-163.
DR PDB; 7RF5; X-ray; 2.23 A; V/v=1-163.
DR PDB; 7RF6; X-ray; 2.01 A; V/v=1-163.
DR PDB; 7RF7; X-ray; 2.09 A; V/v=1-163.
DR PDB; 7RF8; 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 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; P0A386; -.
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; GTCHAGG; -.
DR OrthoDB; 1553768at2; -.
DR EvolutionaryTrace; P0A386; -.
DR Proteomes; UP000000440; Chromosome.
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: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 BINDING 67
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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 BINDING 118
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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:0007829|PDB:1MZ4"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1MZ4"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1MZ4"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1W5C"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:1MZ4"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:1MZ4"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1MZ4"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1MZ4"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 135..152
FT /evidence="ECO:0007829|PDB:1MZ4"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1MZ4"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 160..162
FT /evidence="ECO:0007829|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
