ID A0A0Q4N0Q1_9GAMM Unreviewed; 128 AA.
AC A0A0Q4N0Q1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Cytochrome B562 {ECO:0000313|EMBL:KQN57921.1};
GN ORFNames=ASF13_03775 {ECO:0000313|EMBL:KQN57921.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN57921.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN57921.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57921.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN57921.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57921.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Electron-transport protein of unknown function.
CC {ECO:0000256|ARBA:ARBA00002028}.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQN57921.1}.
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DR EMBL; LMLK01000012; KQN57921.1; -; Genomic_DNA.
DR RefSeq; WP_056235499.1; NZ_LMLK01000012.1.
DR AlphaFoldDB; A0A0Q4N0Q1; -.
DR STRING; 1736225.ASF13_03775; -.
DR Proteomes; UP000050856; 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 Reference proteome {ECO:0000313|Proteomes:UP000050856};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..128
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006227719"
FT BINDING 29
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 124
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 128 AA; 13830 MW; D68A6B55D162732A CRC64;
MRKLLIAMLS STLLFTSVAA LAQDLSADMD VLKGASRTVQ KTDDKAEMVR ALTDMRAAAT
DAKTQTPDKL QGQAADSEQV KQYHGLLDQL IGRIDASLRL ANAGDLAGAK EQAKGFDAIR
NEGHKQFR
//
