CY552_HYDTT
ID CY552_HYDTT Reviewed; 98 AA.
AC P15452; D3DHZ4; E3EUH7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytochrome c-552;
DE AltName: Full=Cytochrome c552;
DE Flags: Precursor;
GN OrderedLocusNames=HTH_0988, Hydth_0984;
OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter.
OX NCBI_TaxID=608538;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1645652; DOI=10.1111/j.1432-1033.1991.tb15979.x;
RA Sanbongi Y., Yang J.H., Igarashi Y., Kodama T.;
RT "Cloning, nucleotide sequence and expression of the cytochrome c-552 gene
RT from Hydrogenobacter thermophilus.";
RL Eur. J. Biochem. 198:7-12(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=20348262; DOI=10.1128/jb.00158-10;
RA Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT "Complete genome sequence of the thermophilic, obligately
RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT thermophilus TK-6.";
RL J. Bacteriol. 192:2651-2652(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=21677850; DOI=10.4056/sigs.1463589;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., Tice H.,
RA Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Ngatchou-Djao O.D., Land M., Hauser L., Jeffries C.D.,
RA Han C., Detter J.C., Ubler S., Rohde M., Tindall B.J., Goker M., Wirth R.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Hydrogenobacter thermophilus type strain (TK-
RT 6).";
RL Stand. Genomic Sci. 4:131-143(2011).
RN [4]
RP PROTEIN SEQUENCE OF 19-98.
RX PubMed=2536668; DOI=10.1128/jb.171.1.65-69.1989;
RA Sanbongi Y., Ishii M., Igarashi Y., Kodama T.;
RT "Amino acid sequence of cytochrome c-552 from a thermophilic hydrogen-
RT oxidizing bacterium, Hydrogenobacter thermophilus.";
RL J. Bacteriol. 171:65-69(1989).
RN [5]
RP THERMOSTABILITY.
RX PubMed=2558725; DOI=10.1021/bi00451a004;
RA Sanbongi Y., Igarashi Y., Kodama T.;
RT "Thermostability of cytochrome c-552 from the thermophilic hydrogen-
RT oxidizing bacterium Hydrogenobacter thermophilus.";
RL Biochemistry 28:9574-9578(1989).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=9657676; DOI=10.1021/bi9803067;
RA Hasegawa J., Yoshida T., Yamazaki T., Sambongi Y., Yu Y., Igarashi Y.,
RA Kodama T., Yamazaki K., Kyogoku Y., Kobayashi Y.;
RT "Solution structure of thermostable cytochrome c-552 from Hydrogenobacter
RT thermophilus determined by 1H-NMR spectroscopy.";
RL Biochemistry 37:9641-9649(1998).
CC -!- FUNCTION: Reacts with hydrogenase.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR EMBL; X57735; CAA40902.1; -; Genomic_DNA.
DR EMBL; AP011112; BAI69446.1; -; Genomic_DNA.
DR EMBL; CP002221; ADO45379.1; -; Genomic_DNA.
DR PIR; S32485; S32485.
DR RefSeq; WP_012963626.1; NC_017161.1.
DR PDB; 1AYG; NMR; -; A=19-98.
DR PDB; 1YNR; X-ray; 2.00 A; A/B/C/D=19-98.
DR PDB; 2AI5; NMR; -; A=19-98.
DR PDB; 3VYM; X-ray; 2.00 A; A=19-98.
DR PDB; 4ZID; X-ray; 1.80 A; A=19-98.
DR PDB; 5AUR; X-ray; 1.26 A; A/C/E/G=19-98.
DR PDB; 5AUS; X-ray; 1.30 A; A/C=19-98.
DR PDBsum; 1AYG; -.
DR PDBsum; 1YNR; -.
DR PDBsum; 2AI5; -.
DR PDBsum; 3VYM; -.
DR PDBsum; 4ZID; -.
DR PDBsum; 5AUR; -.
DR PDBsum; 5AUS; -.
DR AlphaFoldDB; P15452; -.
DR BMRB; P15452; -.
DR SMR; P15452; -.
DR STRING; 608538.HTH_0988; -.
DR EnsemblBacteria; BAI69446; BAI69446; HTH_0988.
DR KEGG; hte:Hydth_0984; -.
DR KEGG; hth:HTH_0988; -.
DR PATRIC; fig|608538.5.peg.1004; -.
DR eggNOG; COG4654; Bacteria.
DR HOGENOM; CLU_133112_1_0_0; -.
DR OMA; MGCHQVD; -.
DR OrthoDB; 1939800at2; -.
DR EvolutionaryTrace; P15452; -.
DR Proteomes; UP000002574; Chromosome.
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 Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002324; Cyt_c_ID.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00606; CYTCHROMECID.
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; Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2536668"
FT CHAIN 19..98
FT /note="Cytochrome c-552"
FT /evidence="ECO:0000269|PubMed:2536668"
FT /id="PRO_0000006531"
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 77
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 HELIX 20..25
FT /evidence="ECO:0007829|PDB:5AUR"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5AUR"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5AUR"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1YNR"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:5AUR"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:5AUR"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:5AUR"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:5AUR"
SQ SEQUENCE 98 AA; 10431 MW; F49713D829DDE927 CRC64;
MKKFLLVAVV GLAGITFANE QLAKQKGCMA CHDLKAKKVG PAYADVAKKY AGRKDAVDYL
AGKIKKGGSG VWGSVPMPPQ NVTDAEAKQL AQWILSIK