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Database: UniProt
Entry: B6ER86_ALISL
LinkDB: B6ER86_ALISL
Original site: B6ER86_ALISL 
ID   B6ER86_ALISL            Unreviewed;       155 AA.
AC   B6ER86;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Cytochrome c {ECO:0000313|EMBL:CAQ81216.1};
GN   OrderedLocusNames=VSAL_II0462 {ECO:0000313|EMBL:CAQ81216.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ81216.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ81216.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ81216.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR000027-2}.
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DR   EMBL; FM178380; CAQ81216.1; -; Genomic_DNA.
DR   RefSeq; WP_012551800.1; NC_011313.1.
DR   AlphaFoldDB; B6ER86; -.
DR   KEGG; vsa:VSAL_II0462; -.
DR   eggNOG; COG3909; Bacteria.
DR   HOGENOM; CLU_106713_4_0_6; -.
DR   Proteomes; UP000001730; Chromosome 2.
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}; Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..155
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002844791"
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         148
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT   BINDING         149
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   155 AA;  17044 MW;  D0124134225943ED CRC64;
     MFTKNNSIKT LIIASTLFAS TSVLAHTFNE ADKAIAYRQA AFTMIAGNVS EMGEMIKGKT
     DWSDAIFSKR ANQLSQLTLM PLDAFYVEGS DKGKTNALPK VWTNFPDFES RLAQFQEDAA
     ALASISDKGD KDAIRKAFGK TVKNCKACHT DYKAK
//
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