CYCP_RHORT
ID CYCP_RHORT Reviewed; 147 AA.
AC P00144; Q2RS39;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytochrome c';
DE Flags: Precursor;
GN OrderedLocusNames=Rru_A2256;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [2]
RP PROTEIN SEQUENCE OF 22-147.
RX PubMed=172499; DOI=10.1016/s0021-9258(19)40774-6;
RA Meyer T.E., Ambler R.P., Bartsch R.G., Kamen M.D.;
RT "Amino acid sequence of cytochrome c' from the purple photosynthetic
RT bacterium Rhodospirillum rubrum S1.";
RL J. Biol. Chem. 250:8416-8421(1975).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-147.
RX PubMed=1316891; DOI=10.1093/oxfordjournals.jbchem.a123756;
RA Yasui M., Harada S., Kai Y., Kasai N., Kusunoki M., Matsuura Y.;
RT "Three-dimensional structure of ferricytochrome c' from Rhodospirillum
RT rubrum at 2.8-A resolution.";
RL J. Biochem. 111:317-324(1992).
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 EMBL; CP000230; ABC23056.1; -; Genomic_DNA.
DR PIR; A00137; CCQFCR.
DR RefSeq; WP_011389911.1; NC_007643.1.
DR RefSeq; YP_427343.1; NC_007643.1.
DR AlphaFoldDB; P00144; -.
DR SMR; P00144; -.
DR STRING; 269796.Rru_A2256; -.
DR EnsemblBacteria; ABC23056; ABC23056; Rru_A2256.
DR KEGG; rru:Rru_A2256; -.
DR PATRIC; fig|269796.9.peg.2354; -.
DR eggNOG; COG3909; Bacteria.
DR HOGENOM; CLU_106713_3_0_5; -.
DR OMA; CRACHDD; -.
DR OrthoDB; 2061303at2; -.
DR PhylomeDB; P00144; -.
DR Proteomes; UP000001929; 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 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 Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:172499"
FT CHAIN 22..147
FT /note="Cytochrome c'"
FT /id="PRO_0000108376"
FT BINDING 137
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT BINDING 140
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT BINDING 141
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"
SQ SEQUENCE 147 AA; 15292 MW; 2B795317D623F21A CRC64;
MKRMMIVAAL AALTTTTVAQ AADPAAYVEY RKSVLSATSN YMKAIGITLK EDLAVPNQTA
DHAKAIASIM ETLPAAFPEG TAGIAKTEAK AAIWKDFEAF KVASKKSQDA ALELASAAET
GDKAAIGAKL QALGGTCKAC HKEFKAD