ID A0A482FEC1_9LAMI Unreviewed; 473 AA. AC A0A482FEC1; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 31-JUL-2019, entry version 3. DE RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00198301}; 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:QBO26887.1}; OS Clinacanthus nutans. OG Plastid; Chloroplast {ECO:0000313|EMBL:QBO26887.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Acanthaceae; Acanthoideae; OC Justicieae; Clinacanthus. OX NCBI_TaxID=714457 {ECO:0000313|EMBL:QBO26887.1}; RN [1] {ECO:0000313|EMBL:QBO26887.1} RP NUCLEOTIDE SEQUENCE. RA Li M., Pei H., Wang J., Zhao K., Zhu Z., Wang H.; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QBO26887.1} RP NUCLEOTIDE SEQUENCE. RA Li M.-N., Pei H.-Q., Wang J.-H., Zhao K.-K., Zhu Z.-X., Wang H.-F.; RT "Complete plastome sequence of Clinacanthus nutans (Acanthaceae): a RT medicinal species in Southern China."; RL Mitochondrial DNA Part B Resour 4:118-119(2019). CC -!- FUNCTION: One of the components of the core complex of photosystem CC II (PSII). It binds chlorophyll and helps catalyze the primary CC light-induced photochemical processes of PSII. PSII is a light- CC driven water:plastoquinone oxidoreductase, using light energy to CC abstract electrons from H(2)O, generating O(2) and a proton CC gradient subsequently used for ATP formation. {ECO:0000256|HAMAP- CC Rule:MF_01496, ECO:0000256|RuleBase:RU004533, CC ECO:0000256|SAAS:SAAS00944813}. CC -!- COFACTOR: CC Note=Binds multiple chlorophylls and provides some of the ligands CC for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may CC also provide a ligand for a Cl- that is required for oxygen CC evolution. PSII binds additional chlorophylls, carotenoids and CC specific lipids. {ECO:0000256|HAMAP-Rule:MF_01496}; CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins CC PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, CC PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral CC proteins of the oxygen-evolving complex and a large number of CC cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP- CC Rule:MF_01496, ECO:0000256|RuleBase:RU004533}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01496, CC 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 ECO:0000256|SAAS:SAAS00569542}. 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; MH778102; QBO26887.1; -; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Acetylation {ECO:0000256|HAMAP-Rule:MF_01496}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944814}; KW Chloroplast {ECO:0000256|RuleBase:RU004533, KW ECO:0000313|EMBL:QBO26887.1}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944827}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|SAAS:SAAS00198307}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944818, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|SAAS:SAAS00198298}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01496}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944815}; KW Photosystem II {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00198310}; KW Plastid {ECO:0000256|RuleBase:RU004533, ECO:0000313|EMBL:QBO26887.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944816, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|SAAS:SAAS00944822, ECO:0000256|SAM:Phobius}. FT TRANSMEM 49 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 136 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 233 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 292 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 425 443 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 367 367 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_01496}. FT METAL 367 367 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 3. {ECO:0000256|HAMAP-Rule: FT MF_01496}. FT MOD_RES 15 15 N-acetylthreonine. {ECO:0000256|HAMAP- FT Rule:MF_01496}. FT MOD_RES 15 15 Phosphothreonine. {ECO:0000256|HAMAP- FT Rule:MF_01496}. SQ SEQUENCE 473 AA; 51930 MW; 2B0FAC5EB988BA3D CRC64; MKILYSLRRF YHVETLFNGT LAVAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVIDTFP YFVSGVLHLI SSAVLGFGGI YHALLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGL GAFLLVFKAL YFGGVYDTWA PGGGDVRKIT NLTLSPSVIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL GSICIFGGIW HILTKPFAWA RRALVWSGEA YLSYSLGALS IFGFTACCFV WFNNTAYPSE FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV SPRSWLATSH FVLGFFFFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN //