9.A.8.1.15
FeoB of 766 aas and 10 TMSs, a potential GTP hydrolysis-driven active transporter or GTP-activated iron uptake channel. The
membrane domain of the trimeric FeoB forms a central pore lined by
highly conserved cysteine residues. This pore aligns with a central pore
in the N-terminal GTPase domain (G-domain) which is lined by aspartyl residues.
Biochemical analyses revealed a putative iron sensor
domain that could connect GTP binding/hydrolysis to the opening of the
pore. Thus, FeoB may be a GTP-gated channel or GTP hydrolysis-driven primary active transporter (Seyedmohammad et al. 2016).
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| Accession Number: | W1MMS7 |
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| Protein Name: | Ferrous iron transport protein B |
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| Length: | 766 |
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| Molecular Weight: | 82470.00 |
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| Species: | Pseudomonas aeruginosa VRFPA03 [1350465] |
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| Number of TMSs: | 11 |
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| Location1 / Topology2 / Orientation3: |
Cell inner membrane1 |
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| Substrate |
iron(2+) |
|---|
1: MTALTLGLIG NPNSGKTTLF NQLTGSRQRV GNWAGVTVER KEGAFHTARH AVRLVDLPGT
61: YSLTSVSAQA SLDEQIACRY IASGEVDVLV NVVDAANLER NLYLTVQLRE MGIPCIVALN
121: MLDIARSQRI RIDIDGLARR LGCPVVPLVS TRADGIDELK AAIDELQVPQ AALAVDYPPA
181: IQAQVGYLLE TRAPAASAIE PRWLALQALE GDIFNGPALG LPPATLEQAR RGCGEEPELA
241: IVDARYRLIG EICAAVCDHQ QAQPHRLTQW LDRVVLNRWL GLPIFLLVMY LMFFFAINIG
301: GALQPIFDKG SSAIFIDGIQ WLGIRFGLPD WLTAFLAQGI GGGVNTVLPL VPQIGLMYLF
361: LSLLEDSGYM ARAAFVMDRL MQALGLPGKS FVPLIVGFGC NVPSIMGART LDAQRERLIT
421: IMMAPFMSCG ARLAIFAVFA GAFFGQGGAL VIFSLYLLGI VVAILTGLLL KHTLMRGEAS
481: PFVMELPLYH VPHLKSLLLQ TWSRLRGFVV RAGKVIILVS LVIGGLNSIT LDGKPVQGDI
541: GHSALASVSQ RLTPLLAPLG VQPDNWQATV GLVTGAMAKE VVVGTLNTLY TAEQIQGEAF
601: DYEGYDLPGQ LRDALVETWD GLVDTFSLSV LANPVEASMA DGDMETGSMG TMASKFGSPI
661: AAYSYLVFVL LYVPCVTAMG AIARESSKGW MAFSVLWGLN VAYSLATLCY QVATFAAHPE
721: RSVLTIAVVL LFNLILMTCL RLFGREQVLQ LPGRMADAPS GQGGCH