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Database: UniProt
Entry: A3N1D3_ACTP2
LinkDB: A3N1D3_ACTP2
Original site: A3N1D3_ACTP2 
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}.
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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
//
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