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Database: UniProt
Entry: A0A127JSU7_9BURK
LinkDB: A0A127JSU7_9BURK
Original site: A0A127JSU7_9BURK 
ID   A0A127JSU7_9BURK        Unreviewed;       152 AA.
AC   A0A127JSU7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Cytochrome C {ECO:0000313|EMBL:AMO22973.1};
GN   ORFNames=UC35_08820 {ECO:0000313|EMBL:AMO22973.1};
OS   Ramlibacter tataouinensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO22973.1, ECO:0000313|Proteomes:UP000070433};
RN   [1] {ECO:0000313|EMBL:AMO22973.1, ECO:0000313|Proteomes:UP000070433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-10 {ECO:0000313|EMBL:AMO22973.1,
RC   ECO:0000313|Proteomes:UP000070433};
RX   PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA   Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT   "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT   description of the genus Ramlibacter.";
RL   Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
CC   -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR000027-2}.
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DR   EMBL; CP010951; AMO22973.1; -; Genomic_DNA.
DR   RefSeq; WP_061498155.1; NZ_CP010951.1.
DR   AlphaFoldDB; A0A127JSU7; -.
DR   PATRIC; fig|94132.3.peg.1796; -.
DR   OrthoDB; 5520910at2; -.
DR   Proteomes; UP000070433; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; 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; 1.20.120.10; Cytochrome c/b562; 1.
DR   InterPro; IPR010980; Cyt_c/b562.
DR   InterPro; IPR002321; Cyt_c_II.
DR   InterPro; IPR012127; Cyt_c_prime.
DR   Pfam; PF01322; Cytochrom_C_2; 1.
DR   PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR   SUPFAM; SSF47175; Cytochromes; 1.
DR   PROSITE; PS51009; CYTCII; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000027-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000027-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000027-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..152
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007449652"
FT   BINDING         142
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT   BINDING         145
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT   BINDING         146
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:PIRSR000027-1"
SQ   SEQUENCE   152 AA;  16092 MW;  14BBA5588643CC5A CRC64;
     MKIAASLAAA AAILAIASPA SAQFAKPEDA VKYRQGSLFV MAQHFGRIGA MVNGRVPYDA
     KAAADNAEVV ADMAKLPWTG FGPGTDKASS PTRAKPEVWS EQIKFKDHAD KMQGETQKLL
     AAAKTNNLDN LKAAFGPTAN SCKACHDAFR KE
//
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