FER_RHORT
ID FER_RHORT Reviewed; 140 AA.
AC Q2RVS1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Encapsulated ferritin-like protein {ECO:0000303|PubMed:27529188};
DE Short=EncFtn {ECO:0000303|PubMed:27529188};
DE EC=1.16.3.1 {ECO:0000269|PubMed:27529188, ECO:0000269|PubMed:32878987};
GN Name=fer {ECO:0000305}; OrderedLocusNames=Rru_A0973;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [2] {ECO:0007744|PDB:5DA5, ECO:0007744|PDB:5L89, ECO:0007744|PDB:5L8B, ECO:0007744|PDB:5L8G}
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 1-96 IN COMPLEX WITH CALCIUM AND
RP IRON, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLU-32; GLU-62 AND HIS-65.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=27529188; DOI=10.7554/elife.18972;
RA He D., Hughes S., Vanden-Hehir S., Georgiev A., Altenbach K., Tarrant E.,
RA Mackay C.L., Waldron K.J., Clarke D.J., Marles-Wright J.;
RT "Structural characterization of encapsulated ferritin provides insight into
RT iron storage in bacterial nanocompartments.";
RL Elife 5:0-0(2016).
RN [3] {ECO:0007744|PDB:5L8F}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-96, AND SUBUNIT.
RA He D., Hughes S., Vanden-Hehir S., Georgiev A., Altenbach K., Tarrant E.,
RA Mackay C.L., Waldron K.J., Clarke D.J., Marles-Wright J.;
RT "Crystal structure of Rhodospirillum rubrum Rru_A0973 mutant E32A, E62A,
RT H65A.";
RL Submitted (JUN-2016) to the PDB data bank.
RN [4] {ECO:0007744|PDB:6SUW, ECO:0007744|PDB:6SV1}
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 1-96, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS OF
RP 31-GLU--GLU-34; GLU-31; GLU-34 AND TRP-38.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=32878987; DOI=10.1074/jbc.ra120.014502;
RA Piergentili C., Ross J., He D., Gallagher K.J., Stanley W.A., Adam L.,
RA Mackay C.L., Basle A., Waldron K.J., Clarke D.J., Marles-Wright J.;
RT "Dissecting the structural and functional roles of a putative metal entry
RT site in encapsulated ferritins.";
RL J. Biol. Chem. 295:15511-15526(2020).
CC -!- FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. A
CC ferritin-like ferroxidase that mineralizes iron inside the encapsulin
CC nanocompartment. Converts Fe(2+) to Fe(3+) that is released to the
CC exterior of the decameric complex for deposition in the encapsulin
CC nanocompartment. In solution the decamer binds 10-15 iron cations; in
CC the encapsulin nanocompartment the decamer can bind up to 48 ions,
CC perhaps via its internal channel and on its exterior. The empty
CC encapsulin nanocompartment sequesters about 2200 Fe ions while the
CC cargo-loaded nanocompartment can maximally sequester about 4150 Fe
CC ions. EncFtn retains ferroxidase activity when encapsulated
CC (PubMed:27529188). Flux in the active site di-iron metal center is
CC thought to be controlled by the 'entry site' of the protein, which both
CC attracts metal and controls the rate of iron oxidation (Probable).
CC Encapsulation in the nanocompartment does not alter either function of
CC this protein (PubMed:32878987). {ECO:0000269|PubMed:27529188,
CC ECO:0000269|PubMed:32878987, ECO:0000305|PubMed:32878987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000269|PubMed:27529188, ECO:0000269|PubMed:32878987};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC Evidence={ECO:0000269|PubMed:27529188, ECO:0000269|PubMed:32878987};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:27529188, ECO:0000269|PubMed:32878987};
CC Note=Binds a di-iron center symmetrically between each dimer. Fe(2+),
CC Zn(2+) and Co(2+) but not Fe(3+), Ca(2+), Mg(2+) or Mn(2+) induce
CC protein oligomerization. {ECO:0000269|PubMed:27529188,
CC ECO:0000269|PubMed:32878987};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:27529188, ECO:0000269|PubMed:32878987};
CC Note=Binds 1 Ca cation symmetrically between each dimer in what is
CC called the entry site; in vivo this may be an Fe cation.
CC {ECO:0000269|PubMed:27529188, ECO:0000269|PubMed:32878987};
CC -!- ACTIVITY REGULATION: Ferroxidase activity inhibited by Zn(2+); mutants
CC at Glu-31, Glu-34 and Trp-38 are also inhibited by Zn(2+).
CC {ECO:0000269|PubMed:32878987}.
CC -!- SUBUNIT: Monomers form antiparallel dimers which assemble in a
CC decameric ring 7 nm in diameter and 4.5 nm thick with a central channel
CC (construct without targeting peptide) (PubMed:27529188, Ref.3,
CC PubMed:32878987). Growth in Fe(2+)-rich medium induces oligomerization,
CC the monomer does not bind metals (PubMed:27529188, PubMed:32878987).
CC The target peptide probably extends away from the ring, to allow
CC binding to the interior of the encapsulin nanocompartment shell
CC (Probable). {ECO:0000269|PubMed:27529188, ECO:0000269|PubMed:32878987,
CC ECO:0000269|Ref.3, ECO:0000305|PubMed:27529188}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:27529188}.
CC -!- SIMILARITY: Belongs to the ferritin-like superfamily. EncFtn family.
CC {ECO:0000305|PubMed:27529188}.
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DR EMBL; CP000230; ABC21774.1; -; Genomic_DNA.
DR RefSeq; WP_011388728.1; NC_007643.1.
DR RefSeq; YP_426061.1; NC_007643.1.
DR PDB; 5DA5; X-ray; 2.06 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-96.
DR PDB; 5L89; X-ray; 2.59 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-96.
DR PDB; 5L8B; X-ray; 2.21 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-96.
DR PDB; 5L8F; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J=1-96.
DR PDB; 5L8G; X-ray; 2.97 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-96.
DR PDB; 6SUW; X-ray; 2.66 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-96.
DR PDB; 6SV1; X-ray; 2.19 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-96.
DR PDBsum; 5DA5; -.
DR PDBsum; 5L89; -.
DR PDBsum; 5L8B; -.
DR PDBsum; 5L8F; -.
DR PDBsum; 5L8G; -.
DR PDBsum; 6SUW; -.
DR PDBsum; 6SV1; -.
DR SMR; Q2RVS1; -.
DR STRING; 269796.Rru_A0973; -.
DR EnsemblBacteria; ABC21774; ABC21774; Rru_A0973.
DR KEGG; rru:Rru_A0973; -.
DR PATRIC; fig|269796.9.peg.1028; -.
DR eggNOG; COG3461; Bacteria.
DR HOGENOM; CLU_161402_0_0_5; -.
DR OMA; NEGYHEP; -.
DR OrthoDB; 1833195at2; -.
DR PhylomeDB; Q2RVS1; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR GO; GO:0004322; F:ferroxidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR030907; Ferrit_encaps.
DR InterPro; IPR009078; Ferritin-like_SF.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR04535; ferrit_encaps; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Encapsulin nanocompartment; Ion transport; Iron;
KW Iron storage; Iron transport; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..140
FT /note="Encapsulated ferritin-like protein"
FT /id="PRO_0000455323"
FT REGION 100..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..140
FT /note="Targeting peptide"
FT /evidence="ECO:0000305|PubMed:27529188"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT BINDING 32
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT BINDING 32
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT BINDING 65
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT BINDING 65
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0000269|PubMed:32878987, ECO:0007744|PDB:5DA5"
FT MUTAGEN 31..34
FT /note="EELE->AELA: Wild-type oligomerization. Increased
FT ferroxidase activity."
FT /evidence="ECO:0000269|PubMed:32878987"
FT MUTAGEN 31
FT /note="E->A: Altered oligomeric state in solution
FT (decamers, tetramers and dimers), partial liganding of
FT metal at this site. Increased ferroxidase activity, alone
FT and encapsulated."
FT /evidence="ECO:0000269|PubMed:32878987"
FT MUTAGEN 32
FT /note="E->A: Forms decamers in the absence of Fe(2+), no
FT bound metal ions, 40% ferroxidase activty."
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0007744|PDB:5L89"
FT MUTAGEN 34
FT /note="E->A: Altered oligomeric state in solution (decamers
FT and dimers), no metal ligand at this site. Increased
FT ferroxidase activity, alone and encapsulated."
FT /evidence="ECO:0000269|PubMed:32878987"
FT MUTAGEN 38
FT /note="W->A,G: Less stable oligomerization, cannot obtain
FT crystals. Increased ferroxidase activity, alone and
FT encapsulated."
FT /evidence="ECO:0000269|PubMed:32878987"
FT MUTAGEN 62
FT /note="E->A: Forms decamers in the absence of Fe(2+), binds
FT 1 Ca(2+) via E-34, loss of ferroxidase activty."
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0007744|PDB:5L8B"
FT MUTAGEN 65
FT /note="H->A: No longer forms decamers in solution, a minor
FT dimeric form is observed, binds 3 Ca(2+), 55% ferroxidase
FT activty."
FT /evidence="ECO:0000269|PubMed:27529188,
FT ECO:0007744|PDB:5L8G"
SQ SEQUENCE 140 AA; 15193 MW; A3CBF7E0604FE6F4 CRC64;
MAQSSNSTHE PLEVLKEETV NRHRAIVSVM EELEAVDWYD QRVDASTDPE LTAILAHNRD
EEKEHAAMTL EWLRRNDAKW AEHLRTYLFT EGPITAIEAA DTAGEGSGGD AAKGATAQGD
GSLGIGSLKG EAALARPPRL
