CYC22_RHOCE
ID CYC22_RHOCE Reviewed; 121 AA.
AC P81154;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cytochrome c2 iso-2;
DE AltName: Full=Cytochrome c552;
OS Rhodospirillum centenum (Rhodocista centenaria).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=34018;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 43720 / DSM 9894 / IAM 14193 / JCM 21060 / NBRC 16667;
RX PubMed=9659396; DOI=10.1016/s0167-4838(98)00030-2;
RA Samyn B., Fitch J., Meyer T.E., Cusanovich M.A., van Beeumen J.J.;
RT "Purification and primary structure analysis of two cytochrome c2 isozymes
RT from the purple phototrophic bacterium Rhodospirillum centenum.";
RL Biochim. Biophys. Acta 1384:345-355(1998).
CC -!- FUNCTION: Cytochrome c2 is found mainly in purple, non-sulfur,
CC photosynthetic bacteria where it functions as the electron donor to the
CC oxidized bacteriochlorophyll in the photophosphorylation pathway.
CC However, it may also have a role in the respiratory chain and is found
CC in some non-photosynthetic bacteria.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +293 mV.;
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR PDB; 1JDL; X-ray; 1.70 A; A=1-121.
DR PDBsum; 1JDL; -.
DR AlphaFoldDB; P81154; -.
DR SMR; P81154; -.
DR EvolutionaryTrace; P81154; -.
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; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002327; Cyt_c_1A/1B.
DR PANTHER; PTHR11961; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Photosynthesis; Transport.
FT CHAIN 1..121
FT /note="Cytochrome c2 iso-2"
FT /id="PRO_0000108342"
FT BINDING 15
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 18
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 19
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 BINDING 98
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 HELIX 5..11
FT /evidence="ECO:0007829|PDB:1JDL"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1JDL"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:1JDL"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1JDL"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1JDL"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1JDL"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:1JDL"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1JDL"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:1JDL"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1JDL"
SQ SEQUENCE 121 AA; 13035 MW; 88939C3C6022430A CRC64;
EDGDPAKGEA VFKKCMACHR VGPDAKNLVG PALTGVIDRQ AGTAPGFNYS AINHAAGEAG
LHWTPENIIA YLPDPNAFLR KFLADAGHAE QAKGSTKMVF KLPDEQERKD VVAYLKQFSP
Q