PETD_MASLA
ID PETD_MASLA Reviewed; 160 AA.
AC P83792; Q5YJJ5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Cytochrome b6-f complex subunit 4 {ECO:0000255|HAMAP-Rule:MF_01344};
DE AltName: Full=17 kDa polypeptide {ECO:0000255|HAMAP-Rule:MF_01344};
DE AltName: Full=Cytochrome b6-f complex subunit IV {ECO:0000303|PubMed:14526088};
GN Name=petD {ECO:0000255|HAMAP-Rule:MF_01344};
OS Mastigocladus laminosus (Fischerella sp.).
OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX NCBI_TaxID=83541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yan J., Zhang H., Cramer W.A.;
RT "Cloning and characterization of the petBD and petCA operon from the
RT thermophilic cyanobacterium Mastigocladus laminosus.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN CYTOCHROME B6-F COMPLEX, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=14526088; DOI=10.1126/science.1090165;
RA Kurisu G., Zhang H., Smith J.L., Cramer W.A.;
RT "Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning
RT the cavity.";
RL Science 302:1009-1014(2003).
CC -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC electron transfer between photosystem II (PSII) and photosystem I
CC (PSI), cyclic electron flow around PSI, and state transitions.
CC {ECO:0000305|PubMed:14526088}.
CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and
CC the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC PetN. The complex functions as a dimer. {ECO:0000269|PubMed:14526088}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000305|PubMed:14526088}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14526088}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. PetD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01344}.
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DR EMBL; AY390357; AAR26243.1; -; Genomic_DNA.
DR PDB; 1VF5; X-ray; 3.00 A; B/O=1-160.
DR PDB; 2D2C; X-ray; 3.80 A; B/O=1-160.
DR PDB; 2E74; X-ray; 3.00 A; B=1-160.
DR PDB; 2E75; X-ray; 3.55 A; B=1-160.
DR PDB; 2E76; X-ray; 3.41 A; B=1-160.
DR PDB; 4H0L; X-ray; 3.25 A; B=1-160.
DR PDB; 4H13; X-ray; 3.07 A; B=1-160.
DR PDB; 4I7Z; X-ray; 2.80 A; B=1-160.
DR PDB; 4PV1; X-ray; 3.00 A; B=1-160.
DR PDBsum; 1VF5; -.
DR PDBsum; 2D2C; -.
DR PDBsum; 2E74; -.
DR PDBsum; 2E75; -.
DR PDBsum; 2E76; -.
DR PDBsum; 4H0L; -.
DR PDBsum; 4H13; -.
DR PDBsum; 4I7Z; -.
DR PDBsum; 4PV1; -.
DR AlphaFoldDB; P83792; -.
DR SMR; P83792; -.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB04646; Dibromothymoquinone.
DR EvolutionaryTrace; P83792; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; 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:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
DR CDD; cd00290; cytochrome_b_C; 1.
DR HAMAP; MF_01344; Cytb6_f_subIV; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005870; Cyt_b6/f_cplx_suIV.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR PIRSF; PIRSF000033; B6f_17K; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR TIGRFAMs; TIGR01156; cytb6/f_IV; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Photosynthesis; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..160
FT /note="Cytochrome b6-f complex subunit 4"
FT /id="PRO_0000061901"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:14526088"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344,
FT ECO:0000305|PubMed:14526088"
FT TOPO_DOM 57..94
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:14526088"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344,
FT ECO:0000305|PubMed:14526088"
FT TOPO_DOM 116..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:14526088"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344,
FT ECO:0000305|PubMed:14526088"
FT TOPO_DOM 152..160
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:14526088"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:4I7Z"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 40..57
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 94..114
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1VF5"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 127..148
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4I7Z"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4I7Z"
SQ SEQUENCE 160 AA; 17674 MW; 3592F24AD0B6F4DE CRC64;
MATLKKPDLS DPKLRAKLAK GMGHNYYGEP AWPNDLLYVF PVVIMGTFAC IVALSVLDPA
MVGEPADPFA TPLEILPEWY LYPVFQILRS VPNKLLGVLL MASVPLGLIL VPFIENVNKF
QNPFRRPVAT TIFLFGTLVT IWLGIGATFP LDKTLTLGLF
