CY552_THET8
ID CY552_THET8 Reviewed; 148 AA.
AC Q5SME3;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cytochrome c-552;
DE AltName: Full=Cytochrome c552;
DE Flags: Precursor;
GN Name=cycA; OrderedLocusNames=TTHA1423;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Keightley J.A., Mather M.W., Fee J.A.;
RT "Molecular cloning, sequence, and expression of cytochrome c552 from
RT Thermus thermophilus.";
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 18-148, AND PYROGLUTAMATE FORMATION AT GLN-18.
RX PubMed=2986626; DOI=10.1016/0006-291x(85)90115-9;
RA Titani K., Ericsson L.H., Hon-Nami K., Miyazawa T.;
RT "Amino acid sequence of cytochrome c-552 from Thermus thermophilus HB8.";
RL Biochem. Biophys. Res. Commun. 128:781-787(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-148.
RX PubMed=11152119; DOI=10.1110/ps.9.11.2074;
RA Fee J.A., Chen Y., Todaro T.R., Bren K.L., Patel K.M., Hill M.G.,
RA Gomez-Moran E., Loehr T.M., Ai J., Thony-Meyer L., Williams P.A., Stura E.,
RA Sridhar V., McRee D.E.;
RT "Integrity of Thermus thermophilus cytochrome c552 synthesized by
RT Escherichia coli cells expressing the host-specific cytochrome c maturation
RT genes, ccmABCDEFGH: biochemical, spectral, and structural characterization
RT of the recombinant protein.";
RL Protein Sci. 9:2074-2084(2000).
CC -!- FUNCTION: This monoheme basic protein appears to function as an
CC electron donor to cytochrome oxidase in T.thermophilus.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; M93437; AAB88580.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71246.1; -; Genomic_DNA.
DR PIR; A00112; CCTW5T.
DR RefSeq; WP_011228671.1; NC_006461.1.
DR RefSeq; YP_144689.1; NC_006461.1.
DR PDB; 1DT1; X-ray; 1.80 A; A=20-148.
DR PDB; 1FOC; X-ray; 3.00 A; A/B=17-148.
DR PDBsum; 1DT1; -.
DR PDBsum; 1FOC; -.
DR AlphaFoldDB; Q5SME3; -.
DR SMR; Q5SME3; -.
DR STRING; 300852.55772805; -.
DR EnsemblBacteria; BAD71246; BAD71246; BAD71246.
DR GeneID; 3169955; -.
DR KEGG; ttj:TTHA1423; -.
DR PATRIC; fig|300852.9.peg.1397; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_093848_3_0_0; -.
DR OMA; ETPMNTT; -.
DR PhylomeDB; Q5SME3; -.
DR EvolutionaryTrace; Q5SME3; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Pyrrolidone carboxylic acid; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2986626"
FT CHAIN 18..148
FT /note="Cytochrome c-552"
FT /id="PRO_0000006533"
FT BINDING 28
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 31
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 32
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 86
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:2986626"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1DT1"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1DT1"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1DT1"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:1DT1"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:1DT1"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1DT1"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1DT1"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1DT1"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:1DT1"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:1DT1"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:1DT1"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1DT1"
SQ SEQUENCE 148 AA; 15974 MW; 6AE7E806BDB5EA1D CRC64;
MKRTLMAFLL LGGLALAQAD GAKIYAQCAG CHQQNGQGIP GAFPPLAGHV AEILAKEGGR
EYLILVLLYG LQGQIEVKGM KYNGVMSSFA QLKDEEIAAV LNHIATAWGD AKKVKGFKPF
TAEEVKKLRA KKLTPQQVLA ERKKLGLK
