ID A0A7T8G4F7_9ERIC Unreviewed; 473 AA. AC A0A7T8G4F7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. DE RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533}; DE AltName: Full=PSII 43 kDa protein {ECO:0000256|HAMAP-Rule:MF_01496}; DE AltName: Full=Protein CP-43 {ECO:0000256|HAMAP-Rule:MF_01496}; GN Name=psbC {ECO:0000256|HAMAP-Rule:MF_01496, GN ECO:0000313|EMBL:QQP21648.1}; OS Vitellaria paradoxa. OG Plastid; Chloroplast {ECO:0000313|EMBL:QQP21648.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Sapotaceae; Sapotoideae; Vitellaria. OX NCBI_TaxID=292385 {ECO:0000313|EMBL:QQP21648.1}; RN [1] {ECO:0000313|EMBL:QQP21648.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=33365563; RA Wang Y., Yuan X., Chen Z., Luo T.; RT "The complete chloroplast genome sequence of Vitellaria paradoxa."; RL Mitochondrial DNA B Resour 4:2403-2404(2019). 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:0000256|HAMAP-Rule:MF_01496, CC ECO:0000256|RuleBase:RU004533}. 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:0000256|HAMAP-Rule:MF_01496}; CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA, CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen- CC evolving complex and a large number of cofactors. It forms dimeric CC complexes. {ECO:0000256|HAMAP-Rule:MF_01496, CC ECO:0000256|RuleBase:RU004533}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01496, CC ECO:0000256|RuleBase:RU004533}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533}. CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MK953548; QQP21648.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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: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 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 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Chloroplast {ECO:0000256|RuleBase:RU004533, ECO:0000313|EMBL:QQP21648.1}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01496}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01496}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Plastid {ECO:0000256|RuleBase:RU004533, ECO:0000313|EMBL:QQP21648.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01496}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01496}. FT CHAIN 15..473 FT /note="Photosystem II CP43 reaction center protein" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01496" FT /id="PRO_5031635550" FT TRANSMEM 49..70 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 111..136 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 157..181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 233..253 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 274..292 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 425..443 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT METAL 367 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01496" FT METAL 367 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01496" FT MOD_RES 15 FT /note="N-acetylthreonine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01496" FT MOD_RES 15 FT /note="Phosphothreonine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01496" SQ SEQUENCE 473 AA; 51806 MW; D9BAD7D7417416FC CRC64; MKTLYSLRRF YPVETLFNGT LALAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVIDTFP YFVSGVLHLI SSAVLGFGGI YHALLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGI GAFLLVFKAL YFGGVYDTWA PGGGDVRKIT NLTLSPSIIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL GSICILGGIW HILTKPFAWA RRALVWSGEA YLSYSLGALS VCGFIACCFV WFNNTAYPSE FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV SPRSWLATSH FVLAFFLFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN //