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5.B.5.2.1
The secreted phototrophic iron (Fe2+) oxidase (CO2 reducing), PioABC (Jiao and Newman, 2007). Photoferrotrophy is a form of anoxygenic photosynthesis whereby bacteria utilize soluble or insoluble forms of ferrous iron as an electron donor to fix carbon dioxide using light energy. They can also use poised electrodes as their electron donor via phototrophic extracellular electron uptake (phototrophic EEU). Gupta et al. 2019 showed that the single periplasmic decaheme cytochrome c, PioA, and the outer membrane porin, PioB, form a complex allowing extracellular electron uptake across the outer membrane from both soluble iron and poised electrodes. They observed that PioA undergoes postsecretory proteolysis of its N terminus to produce a shorter heme-attached PioA (holo-PioAC, where PioAC represents the C terminus of PioA), which can exist both freely in the periplasm and in a complex with PioB. The extended N-terminal peptide controls heme attachment, and its processing is required to produce wild-type levels of the holo-PioAC and holo-PioACB complex. It is also conserved in PioA homologs from other phototrophs (Gupta et al. 2019).

Accession Number:A1EBT4
Protein Name:PioC
Length:94
Molecular Weight:9858.00
Species:Rhodopseudomonas palustris TIE-1 [395960]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate electron

Cross database links:

RefSeq: YP_001989848.1   
Entrez Gene ID: 6408468   
KEGG: rpt:Rpal_0815   

Gene Ontology

GO:0009055 F:electron carrier activity
GO:0019646 P:aerobic electron transport chain

References (1)

[1] “The pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1.”  Jiao Y.et.al.   17189359

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MNDKRNDQPP LSRRKLLKAG VGAAGIAAML GAGVAAANAQ VTKKASHKDA GYQESPNGAK 
61:	RCGTCRQFRP PSSCITVESP ISENGWCRLY AGKA