ID   CYCP_MAGML              Reviewed;         128 AA.
AC   P00152;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cytochrome c';
OS   Magnetospirillum molischianum (Rhodospirillum molischianum).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1083;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Ambler R.P.;
RL   (In) Nichols J.M. (eds.);
RL   Abstracts of the 3rd international symposium on photosynthetic prokaryotes
RL   (Oxford), pp.E17-E17, Univ. Liverpool, Liverpool (1979).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=6279876; DOI=10.1016/0022-2836(81)90286-2;
RA   Weber P.C., Howard A., Xuong N.H., Salemme F.R.;
RT   "Crystallographic structure of Rhodospirillum molischianum ferricytochrome
RT   c' at 2.5-A resolution.";
RL   J. Mol. Biol. 153:399-424(1981).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS).
RX   PubMed=3005592; DOI=10.1016/0022-2836(85)90135-4;
RA   Finzel B.C., Weber P.C., Hardman K.D., Salemme F.R.;
RT   "Structure of ferricytochrome c' from Rhodospirillum molischianum at 1.67-A
RT   resolution.";
RL   J. Mol. Biol. 186:627-643(1985).
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   -!- SUBUNIT: Homodimer.
CC   -!- PTM: Binds 1 heme group per subunit.
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DR   PIR; A00145; CCQFCM.
DR   PDB; 2CCY; X-ray; 1.67 A; A/B=1-128.
DR   PDBsum; 2CCY; -.
DR   AlphaFoldDB; P00152; -.
DR   SMR; P00152; -.
DR   EvolutionaryTrace; P00152; -.
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..128
FT                   /note="Cytochrome c'"
FT                   /id="PRO_0000108374"
FT   BINDING         118
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:3005592"
FT   BINDING         121
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:3005592"
FT   BINDING         122
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:3005592"
FT   HELIX           5..30
FT                   /evidence="ECO:0007829|PDB:2CCY"
FT   HELIX           40..53
FT                   /evidence="ECO:0007829|PDB:2CCY"
FT   HELIX           54..58
FT                   /evidence="ECO:0007829|PDB:2CCY"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:2CCY"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:2CCY"
FT   HELIX           79..102
FT                   /evidence="ECO:0007829|PDB:2CCY"
FT   HELIX           104..125
FT                   /evidence="ECO:0007829|PDB:2CCY"
SQ   SEQUENCE   128 AA;  13421 MW;  9CF7BCE314DD3256 CRC64;
     QQSKPEDLLK LRQGLMQTLK SQWVPIAGFA AGKADLPADA AQRAENMAMV AKLAPIGWAK
     GTEALPNGET KPEAFGSKSA EFLEGWKALA TESTKLAAAA KAGPDALKAQ AAATGKVCKA
     CHEEFKQD