ID A3N1D3_ACTP2 Unreviewed; 124 AA.
AC A3N1D3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Soluble cytochrome b562 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=APL_1129 {ECO:0000313|EMBL:ABN74219.1};
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN74219.1, ECO:0000313|Proteomes:UP000001432};
RN [1] {ECO:0000313|EMBL:ABN74219.1, ECO:0000313|Proteomes:UP000001432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20 {ECO:0000313|EMBL:ABN74219.1,
RC ECO:0000313|Proteomes:UP000001432};
RX PubMed=18065534; DOI=10.1128/JB.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR000029-1};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per molecule.
CC {ECO:0000256|PIRSR:PIRSR000029-1};
CC -!- SIMILARITY: Belongs to the cytochrome b562 family.
CC {ECO:0000256|ARBA:ARBA00005523}.
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; CP000569; ABN74219.1; -; Genomic_DNA.
DR RefSeq; WP_005601602.1; NC_009053.1.
DR AlphaFoldDB; A3N1D3; -.
DR STRING; 416269.APL_1129; -.
DR EnsemblBacteria; ABN74219; ABN74219; APL_1129.
DR GeneID; 69418362; -.
DR KEGG; apl:APL_1129; -.
DR eggNOG; COG3783; Bacteria.
DR HOGENOM; CLU_161963_0_0_6; -.
DR Proteomes; UP000001432; 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; IPR009155; Cyt_b562.
DR InterPro; IPR010980; Cyt_c/b562.
DR Pfam; PF07361; Cytochrom_B562; 1.
DR PIRSF; PIRSF000029; Cytochrome_b562; 1.
DR SUPFAM; SSF47175; Cytochromes; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Heme {ECO:0000256|PIRSR:PIRSR000029-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000029-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000029-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001432};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..124
FT /note="Soluble cytochrome b562"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002655963"
FT COILED 44..103
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 28
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000029-1"
FT BINDING 120
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000029-1"
SQ SEQUENCE 124 AA; 13980 MW; A7B19703FEC18C7F CRC64;
MNKFKQTLAV AMFAFSSVAL ANGVMMEMFQ MNKHMGAFNR AQTAEEFQES AKQFLVQAEK
AKNTMPASLG GDQELFKGYQ AGMQEVIDEV KKAEELAKQD KLEEAKMAVS RLNGLKKKYH
SEYK
//