C556_RHOPA
ID C556_RHOPA Reviewed; 149 AA.
AC P00150;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cytochrome c-556;
DE AltName: Full=Cytochrome c556;
DE Flags: Precursor;
GN OrderedLocusNames=RPA3973;
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 21-149.
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).
CC -!- FUNCTION: Low-spin monoheme cytochrome c.
CC -!- SUBUNIT: Monomer.
CC -!- PTM: Binds 1 heme group per subunit.
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DR EMBL; BX572605; CAE29414.1; -; Genomic_DNA.
DR PIR; A00143; CCRF6P.
DR RefSeq; WP_011159509.1; NC_005296.1.
DR PDB; 1S05; NMR; -; A=21-149.
DR PDBsum; 1S05; -.
DR AlphaFoldDB; P00150; -.
DR SMR; P00150; -.
DR STRING; 258594.RPA3973; -.
DR PRIDE; P00150; -.
DR EnsemblBacteria; CAE29414; CAE29414; RPA3973.
DR GeneID; 66895089; -.
DR KEGG; rpa:RPA3973; -.
DR eggNOG; COG3909; Bacteria.
DR HOGENOM; CLU_106713_2_0_5; -.
DR OMA; HYRQSAF; -.
DR PhylomeDB; P00150; -.
DR BioCyc; RPAL258594:TX73_RS20280-MON; -.
DR EvolutionaryTrace; P00150; -.
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..20
FT /evidence="ECO:0000269|PubMed:6273892"
FT CHAIN 21..149
FT /note="Cytochrome c-556"
FT /id="PRO_0000006548"
FT BINDING 40
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 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"
FT HELIX 25..47
FT /evidence="ECO:0007829|PDB:1S05"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:1S05"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1S05"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1S05"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1S05"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1S05"
FT HELIX 99..119
FT /evidence="ECO:0007829|PDB:1S05"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:1S05"
FT TURN 130..134
FT /evidence="ECO:0007829|PDB:1S05"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:1S05"
SQ SEQUENCE 149 AA; 16149 MW; 6748A28E762AA1C6 CRC64;
MLRTVIVAGA LVLTASAVMA QQDLVDKTQK LMKDNGRNMM VLGAIAKGEK PYDQAAVDAA
LKQFDETAKD LPKLFPDSVK GLKPFDSKYS SSPKIWAERA KFDTEIADFA KAVDGAKGKI
KDVDTLKAAM QPIGKACGNC HENFRDKEG