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Database: UniProt
Entry: D0SRJ2_ACIJU
LinkDB: D0SRJ2_ACIJU
Original site: D0SRJ2_ACIJU 
ID   D0SRJ2_ACIJU            Unreviewed;       129 AA.
AC   D0SRJ2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Cytochrome b562 {ECO:0000313|EMBL:EEY91471.1};
GN   ORFNames=HMPREF0026_03102 {ECO:0000313|EMBL:EEY91471.1};
OS   Acinetobacter junii SH205.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=575587 {ECO:0000313|EMBL:EEY91471.1, ECO:0000313|Proteomes:UP000018442};
RN   [1] {ECO:0000313|Proteomes:UP000018442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH205 {ECO:0000313|Proteomes:UP000018442};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
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; GG705018; EEY91471.1; -; Genomic_DNA.
DR   RefSeq; WP_004914578.1; NZ_GG705018.1.
DR   AlphaFoldDB; D0SRJ2; -.
DR   GeneID; 70090874; -.
DR   HOGENOM; CLU_140814_0_0_6; -.
DR   Proteomes; UP000018442; Unassembled WGS sequence.
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   Heme {ECO:0000256|PIRSR:PIRSR000029-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR000029-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000029-1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..129
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003015348"
FT   BINDING         30
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         125
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   129 AA;  14361 MW;  A954B880E610252A CRC64;
     MKKGFCLATL FASVLMFNQG VSAHQLETDM RVLAKSMTAF AQTQDLAEAK KQLMLMRKAA
     VASKASSPHK LEGVSKDDEQ LKAYQHGLDL LLAQIDSVNA LVEKGQLEQA KVQALELVKL
     RNEYHQQFK
//
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