ID D5WUT8_KYRT2 Unreviewed; 131 AA.
AC D5WUT8;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Cytochrome c class I {ECO:0000313|EMBL:ADG07410.1};
GN OrderedLocusNames=Btus_2763 {ECO:0000313|EMBL:ADG07410.1};
OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG07410.1, ECO:0000313|Proteomes:UP000002368};
RN [1] {ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacillus tusciae DSM 2912.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG07410.1, ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX PubMed=22180816; DOI=10.4056/sigs.2144922;
RA Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA Hugenholtz P., Eisen J.A.;
RT "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT Alicyclobacillaceae da Costa and Rainey, 2010.";
RL Stand. Genomic Sci. 5:121-134(2011).
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000025-1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002017; ADG07410.1; -; Genomic_DNA.
DR RefSeq; WP_013076691.1; NC_014098.1.
DR AlphaFoldDB; D5WUT8; -.
DR STRING; 562970.Btus_2763; -.
DR KEGG; bts:Btus_2763; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_134966_2_0_9; -.
DR OrthoDB; 7933886at2; -.
DR Proteomes; UP000002368; Chromosome.
DR GO; GO:0016020; C:membrane; 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 Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR012218; Cyt_c_BACSU-c550-rel.
DR InterPro; IPR008168; Cyt_C_IC.
DR PANTHER; PTHR37823; CYTOCHROME C-553-LIKE; 1.
DR PANTHER; PTHR37823:SF4; MENAQUINOL-CYTOCHROME C REDUCTASE CYTOCHROME B_C SUBUNIT; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000025; Cytc_Bsub_c550; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000025-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000025-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000025-2}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..131
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038893047"
FT DOMAIN 56..131
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 19..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000025-1"
FT BINDING 72
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000025-1"
FT BINDING 73
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 /evidence="ECO:0000256|PIRSR:PIRSR000025-2"
FT BINDING 108
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 /evidence="ECO:0000256|PIRSR:PIRSR000025-2"
SQ SEQUENCE 131 AA; 12711 MW; 3D1E9CB3E4A2ABCF CRC64;
MKKLLAVLAA GALLVAGCGA ASQPSSGSGS SSASTPTTSS QSGSSSSSSS SSGSGGGSAD
VTALYQQNCQ ACHGANLEGG VGPALDKVGA KLSEDQIQKQ IENGGGTMPG FKSSMKEDDI
KALATWLAAK K
//
