CYC4_THIRO
ID CYC4_THIRO Reviewed; 192 AA.
AC P86052;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Cytochrome c4 {ECO:0000303|PubMed:17931594, ECO:0000303|PubMed:18085548};
OS Thiocapsa roseopersicina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=1058;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, AND HEME-BINDING.
RX PubMed=18085548; DOI=10.1002/jms.1337;
RA Branca R.M.M., Bodo G., Bagyinka C., Prokai L.;
RT "De novo sequencing of a 21-kDa cytochrome c4 from Thiocapsa roseopersicina
RT by nanoelectrospray ionization ion-trap and Fourier-transform ion-cyclotron
RT resonance mass spectrometry.";
RL J. Mass Spectrom. 42:1569-1582(2007).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17931594; DOI=10.1016/j.abb.2007.07.031;
RA Branca R.M.M., Bodo G., Varkonyi Z., Debreczeny M., Oesz J., Bagyinka C.;
RT "Oxygen and temperature-dependent structural and redox changes in a novel
RT cytochrome c(4) from the purple sulfur photosynthetic bacterium Thiocapsa
RT roseopersicina.";
RL Arch. Biochem. Biophys. 467:174-184(2007).
RN [3] {ECO:0000305}
RP CRYSTALLIZATION, AND X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
RX PubMed=16880567; DOI=10.1107/s1744309106027710;
RA Tomcova I., Branca R.M.M., Bodo G., Bagyinka C., Smatanova I.K.;
RT "Cross-crystallization method used for the crystallization and preliminary
RT diffraction analysis of a novel di-haem cytochrome c4.";
RL Acta Crystallogr. F 62:820-824(2006).
CC -!- FUNCTION: Diheme, high potential cytochrome c believed to be an
CC intermediate electron donor in an anaerobic electron transport chain.
CC {ECO:0000269|PubMed:17931594}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=417 nm {ECO:0000269|PubMed:17931594};
CC Note=The absorbance maximum is for the reduced state. The oxidized
CC cytochrome exhibits a weak maximum at 695 nm.;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:17931594}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC {ECO:0000269|PubMed:18085548}.
CC -!- MASS SPECTROMETRY: Mass=20749.0; Method=Electrospray; Note=The measured
CC mass is that of the peptide with a mercury ion coordinated to each heme
CC binding motif.; Evidence={ECO:0000269|PubMed:18085548};
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DR AlphaFoldDB; P86052; -.
DR SMR; P86052; -.
DR STRING; 1058.SAMN05421783_105115; -.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR GO; GO:0015886; P:heme transport; IDA:UniProtKB.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
DR InterPro; IPR024167; Cytochrome_c4-like.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Repeat; Transport.
FT CHAIN 1..192
FT /note="Cytochrome c4"
FT /id="PRO_0000355076"
FT DOMAIN 12..90
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 99..191
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 25
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q52369,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 28
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q52369,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 29
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:0000250|UniProtKB:Q52369,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 120
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q52369,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 123
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q52369,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 124
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:0000250|UniProtKB:Q52369,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 192 AA; 20362 MW; DBA2A84DE8852824 CRC64;
TDGHQAAAPQ VGDPQAGEAK ANGVCLACHG PQGNSLVPIW PKLAGQHPEY IVKQLMDFKQ
RRANEQMTPM AMPLTDQEVL DLAAYYATQP KTPGAADPEL ASKGESLYRW GNPETGVPAC
SGCHGPAGGA GQSLAKFPRL SAQHADYTKQ TLEHFRGALR ANDPNGMMRG AAARLSDQEI
AAVSQYLQGL SQ
