ID   C551_RHOTE              Reviewed;         240 AA.
AC   P83170;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Cytochrome c-551;
OS   Rhodocyclus tenuis (Rhodospirillum tenue).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Rhodocyclus.
OX   NCBI_TaxID=1066 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, HEME-BINDING, AND MASS SPECTROMETRY.
RC   STRAIN=DSM 3761;
RX   PubMed=11019819; DOI=10.1006/abbi.2000.1971;
RA   Devreese B., Brige A., Backers K., Van Driessche G., Meyer T.E.,
RA   Cusanovich M.A., Van Beeumen J.J.;
RT   "Primary structure characterization of a Rhodocyclus tenuis diheme
RT   cytochrome c reveals the existence of two different classes of low-
RT   potential diheme cytochromes c in purple phototropic bacteria.";
RL   Arch. Biochem. Biophys. 381:53-60(2000).
CC   -!- PTM: Binds 2 heme c groups per subunit.
CC   -!- MASS SPECTROMETRY: Mass=26504.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11019819};
CC   -!- MISCELLANEOUS: The second heme binding site has an unusual CXXXCH
CC       motif.
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DR   AlphaFoldDB; P83170; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR019020; Cyt-c552/DMSO_Rdtase_haem-bd.
DR   Pfam; PF09459; EB_dh; 1.
DR   SMART; SM00887; EB_dh; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Repeat; Transport.
FT   CHAIN           1..240
FT                   /note="Cytochrome c-551"
FT                   /id="PRO_0000108420"
FT   BINDING         41
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT   BINDING         44
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT   BINDING         45
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
FT   BINDING         128
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT   BINDING         132
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT   BINDING         133
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   240 AA;  25268 MW;  44A19CEA8588D4C2 CRC64;
     APDWSKIPAR EITVFHAGAT SFEWIGSEHP GASIVKAGQP CIICHETKKG LDYTAKKLAP
     REPDAQAMPK TVSFPVSVQA AVEKGTLNVR LSFKPPADSK TGSDADNELK AAIMLLDIKV
     PQAKLAGCWT SCHKDMRGMP GGDAKKGKYV SAGSFELLQW KSGKTSAALP AGVKVESGKD
     GDRTTVTFSR KLGGAVVEGR SVPFGIAIHA NRAAGRMHYV SLGYRLGIGG APGEVQAAKQ