ID   CYCP_RHOPA              Reviewed;         146 AA.
AC   P00149;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cytochrome c';
DE   Flags: Precursor;
GN   Name=cycA; OrderedLocusNames=RPA2314;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-146.
RC   STRAIN=ATCC 17007 / ATH 2.1.37 / NCIB 11774;
RX   PubMed=6273892; DOI=10.1073/pnas.78.11.6854;
RA   Ambler R.P., Bartsch R.G., Daniel M., Kamen M.D., McLellan L., Meyer T.E.,
RA   van Beeumen J.;
RT   "Amino acid sequences of bacterial cytochromes c' and c-556.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:6854-6857(1981).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=9826513; DOI=10.1006/jmbi.1998.2190;
RA   Shibata N., Iba S., Misaki S., Meyer T.E., Bartsch R.G., Cusanovich M.A.,
RA   Morimoto Y., Higuchi Y., Yasuoka N.;
RT   "Basis for monomer stabilization in Rhodopseudomonas palustris cytochrome
RT   c' derived from the crystal structure.";
RL   J. Mol. Biol. 284:751-760(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS), AND FLUORESCENCE SPECTROSCOPY.
RX   PubMed=12407175; DOI=10.1073/pnas.192574099;
RA   Lee J.C., Engman K.C., Tezcan F.A., Gray H.B., Winkler J.R.;
RT   "Structural features of cytochrome c' folding intermediates revealed by
RT   fluorescence energy-transfer kinetics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14778-14782(2002).
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: Monomer.
CC   -!- PTM: Binds 1 heme group per subunit.
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DR   EMBL; BX572600; CAE27755.1; -; Genomic_DNA.
DR   PIR; A00142; CCRFCP.
DR   RefSeq; WP_011157867.1; NC_005296.1.
DR   PDB; 1A7V; X-ray; 2.30 A; A/B=22-146.
DR   PDB; 1MQV; X-ray; 1.78 A; A/B=22-146.
DR   PDBsum; 1A7V; -.
DR   PDBsum; 1MQV; -.
DR   AlphaFoldDB; P00149; -.
DR   SMR; P00149; -.
DR   STRING; 258594.RPA2314; -.
DR   PRIDE; P00149; -.
DR   EnsemblBacteria; CAE27755; CAE27755; RPA2314.
DR   GeneID; 66893372; -.
DR   KEGG; rpa:RPA2314; -.
DR   eggNOG; COG3909; Bacteria.
DR   HOGENOM; CLU_106713_2_0_5; -.
DR   OMA; ALPKIWD; -.
DR   PhylomeDB; P00149; -.
DR   BioCyc; RPAL258594:TX73_RS11800-MON; -.
DR   EvolutionaryTrace; P00149; -.
DR   Proteomes; UP000001426; Chromosome.
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   Pfam; PF01322; Cytochrom_C_2; 1.
DR   PIRSF; PIRSF000027; Cytc_c_prime; 1.
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; Reference proteome; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:6273892"
FT   CHAIN           22..146
FT                   /note="Cytochrome c'"
FT                   /id="PRO_0000006511"
FT   BINDING         134
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   BINDING         137
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT   BINDING         138
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           25..47
FT                   /evidence="ECO:0007829|PDB:1MQV"
FT   HELIX           55..71
FT                   /evidence="ECO:0007829|PDB:1MQV"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:1MQV"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:1MQV"
FT   HELIX           90..94
FT                   /evidence="ECO:0007829|PDB:1MQV"
FT   HELIX           96..116
FT                   /evidence="ECO:0007829|PDB:1MQV"
FT   HELIX           120..141
FT                   /evidence="ECO:0007829|PDB:1MQV"
SQ   SEQUENCE   146 AA;  15201 MW;  DB09889723E94528 CRC64;
     MKLRIATIAG LVVLGSGFAV AQTDVIAQRK AILKQMGEAT KPIAAMLKGE AKFDQAVVQK
     SLAAIADDSK KLPALFPADS KTGGDTAALP KIWEDKAKFD DLFAKLAAAA TAAQGTIKDE
     ASLKANIGGV LGNCKSCHDD FRAKKS