CYCP_RUBGE
ID CYCP_RUBGE Reviewed; 129 AA.
AC P00142;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome c';
OS Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS gelatinosa).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=28068;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=221823; DOI=10.1038/278661a0;
RA Ambler R.P., Meyer T.E., Kamen M.D.;
RT "Anomalies in amino acid sequences of small cytochromes c and cytochromes
RT c' from two species of purple photosynthetic bacteria.";
RL Nature 278:661-662(1979).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=8380709; DOI=10.1021/bi00054a006;
RA Bertini I., Gori G., Luchinat C., Vila A.J.;
RT "One- and two-dimensional NMR characterization of oxidized and reduced
RT cytochrome c' from Rhodocyclus gelatinosus.";
RL Biochemistry 32:776-783(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RA Archer M., Banci L., Dikaya E., Romao M.J.;
RT "Crystal structure of cytochrome c' from Rhodocyclus gelatinosus and
RT comparison with other cytochromes c'.";
RL J. Biol. Inorg. Chem. 2:611-622(1997).
CC -!- FUNCTION: Cytochrome c' is the most widely occurring bacterial c-type
CC cytochrome. Cytochromes c' are high-spin proteins and the heme has no
CC sixth ligand. Their exact function is not known.
CC -!- PTM: Binds 1 heme group per subunit.
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DR PIR; A00135; CCRFCG.
DR PDB; 1JAF; X-ray; 2.50 A; A/B=1-129.
DR PDB; 2J8W; X-ray; 1.29 A; A/B=1-129.
DR PDB; 2J9B; X-ray; 1.50 A; A/B=1-129.
DR PDBsum; 1JAF; -.
DR PDBsum; 2J8W; -.
DR PDBsum; 2J9B; -.
DR AlphaFoldDB; P00142; -.
DR SMR; P00142; -.
DR EvolutionaryTrace; P00142; -.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR InterPro; IPR010980; Cyt_c/b562.
DR InterPro; IPR002321; Cyt_c_II.
DR InterPro; IPR012127; Cyt_c_prime.
DR InterPro; IPR015984; Cyt_c_prime_subgr.
DR Pfam; PF01322; Cytochrom_C_2; 1.
DR PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR PRINTS; PR00608; CYTCHROMECII.
DR SUPFAM; SSF47175; SSF47175; 1.
DR PROSITE; PS51009; CYTCII; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Transport.
FT CHAIN 1..129
FT /note="Cytochrome c'"
FT /id="PRO_0000108373"
FT BINDING 119
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT BINDING 122
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT BINDING 123
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 HELIX 5..30
FT /evidence="ECO:0007829|PDB:2J8W"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2J8W"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2J8W"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2J9B"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2J9B"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2J8W"
FT HELIX 79..102
FT /evidence="ECO:0007829|PDB:2J8W"
FT HELIX 105..126
FT /evidence="ECO:0007829|PDB:2J8W"
SQ SEQUENCE 129 AA; 13283 MW; 05E262B64588ACB7 CRC64;
QFQKPGDAIE YRQSAFTLIA NHFGRVAAMA QGKAPFDAKV AAENIALVST LSKLPLTAFG
PGTDKGHGTE AKPAVWSDAA GFKAAADKFA AAVDKLDAAG KTGDFAQIKA AVGETGGACK
GCHDKFKEK
