CY551_CHLTE
ID CY551_CHLTE Reviewed; 206 AA.
AC O07091;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytochrome c;
DE AltName: Full=Cytochrome c-z {ECO:0000303|PubMed:20156447};
DE Short=Cyt c-z {ECO:0000303|PubMed:20156447};
DE AltName: Full=Photosystem P840 reaction center cytochrome c-551;
GN Name=pscC; OrderedLocusNames=CT1639;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9230061; DOI=10.1021/bi9701787;
RA Oh-oka H., Iwaki M., Itoh S.;
RT "Viscosity dependence of the electron transfer rate from bound cytochrome c
RT to P840 in the photosynthetic reaction center of the green sulfur bacterium
RT Chlorobium tepidum.";
RL Biochemistry 36:9267-9272(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=10976061; DOI=10.1126/science.289.5485.1724;
RA Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.;
RT "Molecular evidence for the early evolution of photosynthesis.";
RL Science 289:1724-1730(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [4]
RP ELECTRON MICROSCOPY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10398586; DOI=10.1006/jmbi.1999.2925;
RA Remigy H.W., Stahlberg H., Fotiadis D., Mueller S.A., Wolpensinger B.,
RA Engel A., Hauska G., Tsiotis G.;
RT "The reaction center complex from the green sulfur bacterium Chlorobium
RT tepidum: a structural analysis by scanning transmission electron
RT microscopy.";
RL J. Mol. Biol. 290:851-858(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 117-206 IN COMPLEX WITH HEME,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PTM.
RX PubMed=20156447; DOI=10.1016/j.jmb.2010.02.011;
RA Hirano Y., Higuchi M., Azai C., Oh-Oka H., Miki K., Wang Z.Y.;
RT "Crystal structure of the electron carrier domain of the reaction center
RT cytochrome c(z) subunit from green photosynthetic bacterium Chlorobium
RT tepidum.";
RL J. Mol. Biol. 397:1175-1187(2010).
CC -!- FUNCTION: Monoheme cytochrome which is the immediate electron donor to
CC P840 of the photosynthetic reaction center complex.
CC {ECO:0000269|PubMed:9230061}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +188 mV for the C-terminal domain (117-206) of cytochrome c
CC (at pH 7.0). {ECO:0000269|PubMed:20156447};
CC -!- SUBUNIT: Monomer (PubMed:20156447). Component of the photosynthetic
CC reaction center composed of protein subunits PscA, PscC, PscB and PscD.
CC The reaction center interacts with FmoA (which forms the Fenna-
CC Matthews-Olson (FMO) complex). The reaction center/FmoA complex has two
CC PscA subunits, one PscB and one PscD subunit, probably two FmoA
CC complexes and at least one PscC subunit (PubMed:10398586).
CC {ECO:0000269|PubMed:10398586, ECO:0000269|PubMed:20156447}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:10398586}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- PTM: Binds 1 heme group per subunit. {ECO:0000269|PubMed:20156447}.
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DR EMBL; AB004460; BAA20402.1; -; Genomic_DNA.
DR EMBL; AF287481; AAG12197.1; -; Genomic_DNA.
DR EMBL; AE006470; AAM72864.1; -; Genomic_DNA.
DR RefSeq; NP_662522.1; NC_002932.3.
DR RefSeq; WP_010933303.1; NC_002932.3.
DR PDB; 3A9F; X-ray; 1.30 A; A/B=117-206.
DR PDBsum; 3A9F; -.
DR AlphaFoldDB; O07091; -.
DR SMR; O07091; -.
DR STRING; 194439.CT1639; -.
DR EnsemblBacteria; AAM72864; AAM72864; CT1639.
DR KEGG; cte:CT1639; -.
DR PATRIC; fig|194439.7.peg.1482; -.
DR eggNOG; COG3245; Bacteria.
DR HOGENOM; CLU_1293374_0_0_10; -.
DR OMA; TKYKKTG; -.
DR OrthoDB; 1450807at2; -.
DR EvolutionaryTrace; O07091; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR019604; Cytochrome-c551.
DR Pfam; PF10643; Cytochrome-c551; 1.
DR PIRSF; PIRSF000009; Cytochrome_c551; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Electron transport; Heme;
KW Iron; Membrane; Metal-binding; Photosynthesis; Reaction center;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..206
FT /note="Cytochrome c"
FT /id="PRO_0000108388"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:20156447,
FT ECO:0007744|PDB:3A9F"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:20156447,
FT ECO:0007744|PDB:3A9F"
FT BINDING 156
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20156447,
FT ECO:0007744|PDB:3A9F"
FT BINDING 182
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20156447,
FT ECO:0007744|PDB:3A9F"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:3A9F"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3A9F"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3A9F"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:3A9F"
FT TURN 169..173
FT /evidence="ECO:0007829|PDB:3A9F"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:3A9F"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:3A9F"
SQ SEQUENCE 206 AA; 22715 MW; BDA32D99BE39D2EC CRC64;
MDKNSNGKLI ALAVGGAVLM GALFFSVSFL TGYIPAPNHS AILTPLRSFM GWFLLIFCAS
IIIMGLGKMS SAISDKWFLS FPLSIFVIVM VMFLSLRVYW EKGRTTTVDG KYIRTTAELK
EFLNKPAATS DVPPAPAGFD FDAAKKLVDV RCNKCHTLDS VADLFRTKYK KTGQVNLIVK
RMQGFPGSGI SDDDAKTIGI WLHEKF
