FESII_AZOVI
ID FESII_AZOVI Reviewed; 122 AA.
AC Q44501;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein FeSII {ECO:0000303|PubMed:5668181};
DE Short=FeSII;
DE AltName: Full=Shethna protein FeSII {ECO:0000303|PubMed:26654855};
GN Name=fesII {ECO:0000303|PubMed:7830548};
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=CA;
RX PubMed=7830548; DOI=10.1111/j.1365-2958.1994.tb01270.x;
RA Moshiri F., Kim J.W., Fu C., Maier R.J.;
RT "The FeSII protein of Azotobacter vinelandii is not essential for aerobic
RT nitrogen fixation, but confers significant protection to oxygen-mediated
RT inactivation of nitrogenase in vitro and in vivo.";
RL Mol. Microbiol. 14:101-114(1994).
RN [2]
RP PROTEIN IDENTIFICATION, AND COFACTOR.
RC STRAIN=CA;
RX PubMed=5668181; DOI=10.1016/0006-291x(68)90531-7;
RA Shethna Y.I., DerVartanian D.V., Beinert H.;
RT "Non heme (iron-sulfur) proteins of Azotobacter vinelandii.";
RL Biochem. Biophys. Res. Commun. 31:862-868(1968).
RN [3]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=CA;
RX PubMed=7548055; DOI=10.1021/bi00040a007;
RA Moshiri F., Crouse B.R., Johnson M.K., Maier R.J.;
RT "The 'nitrogenase-protective' FeSII protein of Azotobacter vinelandii:
RT overexpression, characterization, and crystallization.";
RL Biochemistry 34:12973-12982(1995).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-13; 15-LYS-LYS-16;
RP LYS-15; LYS-16 AND HIS-56.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW, and CA;
RX PubMed=10220344; DOI=10.1021/bi9827823;
RA Lou J., Moshiri F., Johnson M.K., Lafferty M.E., Sorkin D.L., Miller A.,
RA Maier R.J.;
RT "Mutagenesis studies of the FeSII protein of Azotobacter vinelandii: roles
RT of histidine and lysine residues in the protection of nitrogenase from
RT oxygen damage.";
RL Biochemistry 38:5563-5571(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS).
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RA Kabasakal B., Cotton C.A.R., Lieber L., Murray J.W.;
RT "Structure of Fesi protein from Azotobacter vinelandii.";
RL Submitted (DEC-2015) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS), FUNCTION, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 70-LYS-GLU-71.
RX PubMed=26654855; DOI=10.1021/jacs.5b10341;
RA Schlesier J., Rohde M., Gerhardt S., Einsle O.;
RT "A conformational switch triggers nitrogenase protection from oxygen damage
RT by Shethna protein II (FeSII).";
RL J. Am. Chem. Soc. 138:239-247(2016).
CC -!- FUNCTION: Binds to and protects nitrogenase from irreversible exposure
CC to O(2), in what is known as 'conformational protection'
CC (PubMed:7830548, PubMed:7548055, PubMed:10220344, PubMed:26654855).
CC Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2
CC states, an open oxidized state that binds and protects nitrogenase, and
CC a closed reduced state that probably does not bind nitrogenase;
CC cooperative oxidation of the 2Fe-2S clusters causes the conformation
CC change (PubMed:26654855). Does not protect nitrogenase with the
CC vanadium-iron subunit, not clear if it protects the iron-only
CC nitrogenase (PubMed:7830548). {ECO:0000269|PubMed:10220344,
CC ECO:0000269|PubMed:26654855, ECO:0000269|PubMed:7548055,
CC ECO:0000269|PubMed:7830548}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465,
CC ECO:0000269|PubMed:26654855, ECO:0000269|PubMed:5668181,
CC ECO:0000269|PubMed:7548055};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00465, ECO:0000269|PubMed:26654855,
CC ECO:0000269|PubMed:7548055};
CC -!- SUBUNIT: Homodimer (PubMed:7548055, PubMed:26654855). Forms a complex
CC with nitrogenase consisting of 1 MoFe heterotetramer, 1 Fe protein
CC dimer and 1 FeSII dimer; the interaction is electrostatic and disurpted
CC by increasing NaCl levels (PubMed:26654855).
CC {ECO:0000269|PubMed:26654855, ECO:0000269|PubMed:7548055}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:26654855}.
CC -!- INDUCTION: Expressed in nitrogen-fixing and non-nitrogen-fixing cells,
CC although transcript levels are higher in nitrogen-fixing cells.
CC Expressed during log and stationary phase growth (at protein level).
CC The gene is monocistronic (PubMed:7830548).
CC {ECO:0000269|PubMed:7830548}.
CC -!- DOMAIN: Has mobile N-loop (residues 59-96) that changes position in a
CC redox-dependent manner being folded against the protein in the closed
CC reduced state, protecting its [2Fe-2S] cluster, or away from the
CC protein in the open oxidized state. The open form complexes with the
CC MoFe and Fe subunits of nitrogenase protecting them from O(2)
CC (PubMed:26654855). {ECO:0000269|PubMed:26654855}.
CC -!- DISRUPTION PHENOTYPE: No visible growth phenotype, but shortly after
CC entry into stationary phase the nitrogenase subunitsare destabilized
CC and are no longer detectable (PubMed:7830548). In vitro nitrogenase is
CC highly sensitive to O(2) (PubMed:7830548, PubMed:10220344).
CC {ECO:0000269|PubMed:10220344, ECO:0000269|PubMed:7830548}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305|PubMed:26654855}.
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DR EMBL; L25896; AAA99834.1; -; Genomic_DNA.
DR PIR; I39741; I39741.
DR RefSeq; WP_012702484.1; NZ_FPKM01000003.1.
DR PDB; 5FFI; X-ray; 2.17 A; A/B/C/D/E=1-122.
DR PDB; 5FRT; X-ray; 2.34 A; A/B/C/D/E=1-122.
DR PDB; 6YAV; X-ray; 1.65 A; A/B/C/D/E=1-122.
DR PDBsum; 5FFI; -.
DR PDBsum; 5FRT; -.
DR PDBsum; 6YAV; -.
DR AlphaFoldDB; Q44501; -.
DR SMR; Q44501; -.
DR OMA; WRLACQM; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW Iron; Iron-sulfur; Metal-binding; Nitrogen fixation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7830548"
FT CHAIN 2..122
FT /note="Protein FeSII"
FT /id="PRO_0000437155"
FT DOMAIN 2..119
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT REGION 59..96
FT /note="N-loop"
FT /evidence="ECO:0000305|PubMed:26654855"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:26654855"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:26654855"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:26654855"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:26654855"
FT MUTAGEN 13
FT /note="H->Q: Wild-type protection of nitrogenase."
FT /evidence="ECO:0000269|PubMed:10220344"
FT MUTAGEN 15..16
FT /note="KK->AA: Considerably decreased protection of
FT nitrogenase, in vivo no nitrogenase is detected once cells
FT reach stationary phase."
FT /evidence="ECO:0000269|PubMed:10220344"
FT MUTAGEN 15
FT /note="K->A: Decreased protection of nitrogenase."
FT /evidence="ECO:0000269|PubMed:10220344"
FT MUTAGEN 16
FT /note="K->A: Decreased protection of nitrogenase."
FT /evidence="ECO:0000269|PubMed:10220344"
FT MUTAGEN 56
FT /note="H->Q: Considerably decreased protection of
FT nitrogenase."
FT /evidence="ECO:0000269|PubMed:10220344"
FT MUTAGEN 70..71
FT /note="KE->AA: No longer protects nitrogenase."
FT /evidence="ECO:0000269|PubMed:26654855"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6YAV"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:6YAV"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5FRT"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:6YAV"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6YAV"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:6YAV"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:6YAV"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:6YAV"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6YAV"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6YAV"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6YAV"
SQ SEQUENCE 122 AA; 13271 MW; BA47D92C4B5EAABC CRC64;
MATIYFSSPL MPHNKKVQAV AGKRSTLLGV AQENGVKIPF ECQDGNCGSC LVKITHLDGE
RIKGMLLTDK ERNVLKSVGK LPKSEEERAA VRDLPPTYRL ACQTIVTDED LLVEFTGEPG
GA
