IMEF_QUATH
ID IMEF_QUATH Reviewed; 192 AA.
AC A0A0F5HNH9; A0A0F5ID09;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Ferritin-like protein {ECO:0000303|PubMed:31282860};
DE EC=1.16.3.1 {ECO:0000269|PubMed:31282860, ECO:0000305|PubMed:31194509};
DE AltName: Full=IMEF cargo protein {ECO:0000303|PubMed:28263314};
GN Name=IMEF {ECO:0000303|PubMed:28263314}; ORFNames=QY95_01593;
OS Quasibacillus thermotolerans.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Quasibacillus.
OX NCBI_TaxID=1221996;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTCC 10057 / 5.5LF 38TD, and MTCC 8252;
RX PubMed=28947104; DOI=10.1016/j.syapm.2017.07.010;
RA Verma A., Pal Y., Khatri I., Ojha A.K., Gruber-Vodicka H., Schumann P.,
RA Dastager S., Subramanian S., Mayilraj S., Krishnamurthi S.;
RT "Examination into the taxonomic position of Bacillus thermotolerans Yang et
RT al., 2013, proposal for its reclassification into a new genus and species
RT Quasibacillus thermotolerans gen. nov., comb. nov. and reclassification of
RT B. encimensis Dastager et al., 2015 as a later heterotypic synonym of B.
RT badius.";
RL Syst. Appl. Microbiol. 40:411-422(2017).
RN [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP 183-LYS--GLN-192.
RC STRAIN=MTCC 10057 / 5.5LF 38TD;
RX PubMed=28263314; DOI=10.1038/nmicrobiol.2017.29;
RA Giessen T.W., Silver P.A.;
RT "Widespread distribution of encapsulin nanocompartments reveals functional
RT diversity.";
RL Nat. Microbiol. 2:17029-17029(2017).
RN [3]
RP FUNCTION, PROBABLE CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP BIOTECHNOLOGY.
RX PubMed=31194509; DOI=10.1021/acsnano.9b03140;
RA Sigmund F., Pettinger S., Kube M., Schneider F., Schifferer M.,
RA Schneider S., Efremova M.V., Pujol-Marti J., Aichler M., Walch A.,
RA Misgeld T., Dietz H., Westmeyer G.G.;
RT "Iron-Sequestering Nanocompartments as Multiplexed Electron Microscopy Gene
RT Reporters.";
RL ACS Nano 13:8114-8123(2019).
RN [4] {ECO:0007744|PDB:6N63}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH FE(3+), FUNCTION,
RP POSSIBLE CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 180-HIS--GLN-192.
RC STRAIN=MTCC 8252;
RX PubMed=31282860; DOI=10.7554/elife.46070;
RA Giessen T.W., Orlando B.J., Verdegaal A.A., Chambers M.G., Gardener J.,
RA Bell D.C., Birrane G., Liao M., Silver P.A.;
RT "Large protein organelles form a new iron sequestration system with high
RT storage capacity.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. A
CC ferritin-like iron-binding protein probably involved in iron
CC mineralization in the encapsulin nanocompartment. Has ferroxidase
CC activity even when encapsulated, the rate is probably controlled by the
CC rate of Fe flux across the nanocompartment pores (PubMed:31282860).
CC Part of the iron-mineralizing encapsulin-associated Firmicute (IMEF)
CC system. 2 different cargo proteins have been identified (IMEF and Fer);
CC when both are expressed in E.coli with the shell protein only IMEF is
CC detected within the nanocompartment. E.coli expressing all 3 genes
CC stores the largest amount of iron and is protected from Fe/H2O2-induced
CC oxidative stress (PubMed:28263314). {ECO:0000269|PubMed:28263314,
CC ECO:0000269|PubMed:31282860}.
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:31282860, ECO:0000305|PubMed:31194509};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC Evidence={ECO:0000269|PubMed:31282860};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC The empty encapsulin nanocompartment is stable until 86.6 degrees
CC Celsius, when loaded with cargo protein is stable until 88.9 degrees
CC Celsius and when grown in high-iron conditions is stable until 91.8
CC degrees Celsius. {ECO:0000269|PubMed:31282860};
CC -!- SUBUNIT: Homodimer, with 2 Fe atoms bound at the subunit interface
CC (without encapsulin), probably also a dimer when encapsulated. 42
CC electron-dense accretions can be seen inside the nanocompartment which
CC are probably this cargo protein, although perhaps up to one cargo dimer
CC can be bound per shell protein. {ECO:0000269|PubMed:31282860,
CC ECO:0000305|PubMed:28263314}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:31194509, ECO:0000269|PubMed:31282860}.
CC -!- DOMAIN: The C-terminus (targeting peptide) is probably responsible for
CC targeting to the encapsulin nanocompartment; it is separated from the
CC rest of the protein by a flexible 37-residue linker.
CC {ECO:0000305|PubMed:28263314, ECO:0000305|PubMed:31282860}.
CC -!- BIOTECHNOLOGY: The encapsulin and cargo pair can be overexpressed in
CC E.coli and in human HEK293T cells. In HEK293T in the presence of 0.5 M
CC ferrous ammonium sulfate nanocompartments can be detected and used as
CC cell markers. Can also be targeted to cell membranes by addition of a
CC farnesylation signal to its C-terminus. Coexpression of this
CC nanocompartment with a smaller nanocompartment from M.xanthus (AC
CC Q1D6H4) allows of expression of different sized iron-rich particles.
CC The encapsulin shell proteins are not seen to mix.
CC {ECO:0000269|PubMed:31194509}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JWIR02000003; KKB43348.1; -; Genomic_DNA.
DR RefSeq; WP_039238473.1; NZ_JWJE02000035.1.
DR PDB; 6N63; X-ray; 1.72 A; A=1-192.
DR PDBsum; 6N63; -.
DR SMR; A0A0F5HNH9; -.
DR STRING; 1221996.QY95_01593; -.
DR EnsemblBacteria; KKB43348; KKB43348; QY95_01593.
DR OrthoDB; 1561204at2; -.
DR Proteomes; UP000031563; Unassembled WGS sequence.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR GO; GO:0004322; F:ferroxidase activity; IDA:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR030909; Geobac_encap.
DR TIGRFAMs; TIGR04536; geobac_encap; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Encapsulin nanocompartment; Iron; Iron storage;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..192
FT /note="Ferritin-like protein"
FT /id="PRO_0000455333"
FT REGION 143..179
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:31282860"
FT REGION 149..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..192
FT /note="Targeting peptide"
FT /evidence="ECO:0000269|PubMed:31282860"
FT COMPBIAS 149..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:31282860,
FT ECO:0007744|PDB:6N63"
FT BINDING 48
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:31282860,
FT ECO:0007744|PDB:6N63"
FT BINDING 102
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:31282860,
FT ECO:0007744|PDB:6N63"
FT MUTAGEN 180..192
FT /note="Missing: No longer targeted to encapsulin
FT nanocompartment."
FT /evidence="ECO:0000269|PubMed:31282860"
FT MUTAGEN 183..192
FT /note="Missing: No longer targeted to encapsulin
FT nanocompartment."
FT /evidence="ECO:0000269|PubMed:28263314"
SQ SEQUENCE 192 AA; 22608 MW; 4B0941B5BC64E410 CRC64;
MKEELDAFHQ IFTTTKEAIE RFMAMLTPVI ENAEDDHERL YYHHIYEEEE QRLSRLDVLI
PLIEKFQDET DEGLFSPSNN AFNRLLQELN LEKFGLHNFI EHVDLALFSF TDEERQTLLK
ELRKDAYEGY QYVKEKLAEI NARFDHDYAD PHAHHDEHRD HLADMPSAGS SHEEVQPVAH
KKKGFTVGSL IQ
