FLP_THEMA
ID FLP_THEMA Reviewed; 114 AA.
AC Q9WZP3; G4FD38;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ferritin-like protein {ECO:0000303|PubMed:19172747};
DE Short=Flp {ECO:0000303|PubMed:19172747};
DE AltName: Full=Encapsulin-associated ferritin-like protein;
GN OrderedLocusNames=TM_0786;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=27224728; DOI=10.1021/acs.biochem.6b00294;
RA Cassidy-Amstutz C., Oltrogge L., Going C.C., Lee A., Teng P.,
RA Quintanilla D., East-Seletsky A., Williams E.R., Savage D.F.;
RT "Identification of a Minimal Peptide Tag for in Vivo and in Vitro Loading
RT of Encapsulin.";
RL Biochemistry 55:3461-3468(2016).
RN [3]
RP SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=30376298; DOI=10.1021/acssynbio.8b00295;
RA Williams E.M., Jung S.M., Coffman J.L., Lutz S.;
RT "Pore Engineering for Enhanced Mass Transport in Encapsulin
RT Nanocompartments.";
RL ACS Synth. Biol. 7:2514-2517(2018).
RN [4]
RP SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RX PubMed=32961724; DOI=10.3390/biom10091342;
RA Xiong X., Sun C., Vago F.S., Klose T., Zhu J., Jiang W.;
RT "Cryo-EM Structure of Heterologous Protein Complex Loaded Thermotoga
RT Maritima Encapsulin Capsid.";
RL Biomolecules 10:0-0(2020).
RN [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=34815415; DOI=10.1038/s41598-021-01932-w;
RA LaFrance B.J., Cassidy-Amstutz C., Nichols R.J., Oltrogge L.M., Nogales E.,
RA Savage D.F.;
RT "The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry
RT matched ferritin-like cargo protein.";
RL Sci. Rep. 11:22810-22810(2021).
RN [6] {ECO:0007744|PDB:3DKT}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 106-113, FUNCTION, PROBABLE IRON
RP COFACTOR, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=19172747; DOI=10.1038/nsmb.1473;
RA Sutter M., Boehringer D., Gutmann S., Gunther S., Prangishvili D.,
RA Loessner M.J., Stetter K.O., Weber-Ban E., Ban N.;
RT "Structural basis of enzyme encapsulation into a bacterial
RT nanocompartment.";
RL Nat. Struct. Mol. Biol. 15:939-947(2008).
CC -!- FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. A
CC ferritin-like protein that probably stores iron in the encapsulin
CC nanocompartment. {ECO:0000305|PubMed:19172747}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000305|PubMed:19172747};
CC -!- SUBUNIT: Probably forms a decamer which binds to the pentameric axis of
CC the interior of the protein shell; as the Flp cargo protein is
CC flexible, packing into the shell is not rigid.
CC {ECO:0000305|PubMed:34815415}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:19172747, ECO:0000269|PubMed:27224728,
CC ECO:0000269|PubMed:30376298, ECO:0000269|PubMed:32961724,
CC ECO:0000269|PubMed:34815415}.
CC -!- DOMAIN: The C-terminal 15-30 residues (cargo loading-peptide, CLP, or
CC targeting peptide) are sufficient to target this protein to the
CC nanocompartment in vivo, while the C-terminal 5 residues suffice in
CC vitro. {ECO:0000269|PubMed:27224728, ECO:0000269|PubMed:30376298,
CC ECO:0000269|PubMed:32961724, ECO:0000305|PubMed:19172747}.
CC -!- BIOTECHNOLOGY: The 15 or 30 C-terminal residues can be used to target
CC foreign proteins to the nanocompartment. {ECO:0000269|PubMed:27224728,
CC ECO:0000269|PubMed:30376298, ECO:0000269|PubMed:32961724}.
CC -!- SIMILARITY: Belongs to the ferritin-like superfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35868.1; -; Genomic_DNA.
DR PIR; C72333; C72333.
DR RefSeq; NP_228595.1; NC_000853.1.
DR RefSeq; WP_004080895.1; NZ_CP011107.1.
DR PDB; 3DKT; X-ray; 3.10 A; K/L/M/N/O/P/Q/R/S/T=106-113.
DR PDBsum; 3DKT; -.
DR SMR; Q9WZP3; -.
DR IntAct; Q9WZP3; 1.
DR STRING; 243274.THEMA_00720; -.
DR EnsemblBacteria; AAD35868; AAD35868; TM_0786.
DR KEGG; tma:TM0786; -.
DR KEGG; tmw:THMA_0805; -.
DR PATRIC; fig|243274.17.peg.788; -.
DR OMA; NEGYHEP; -.
DR OrthoDB; 1833195at2; -.
DR EvolutionaryTrace; Q9WZP3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0140737; C:encapsulin nanocompartment; 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 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; Encapsulin nanocompartment; Iron; Iron storage;
KW Metal-binding; Reference proteome.
FT CHAIN 1..114
FT /note="Ferritin-like protein"
FT /id="PRO_0000455324"
FT REGION 86..114
FT /note="Cargo-loading peptide"
FT /evidence="ECO:0000269|PubMed:27224728,
FT ECO:0000269|PubMed:30376298, ECO:0000269|PubMed:32961724,
FT ECO:0000305|PubMed:19172747"
FT REGION 94..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 29
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
SQ SEQUENCE 114 AA; 13289 MW; BD3DF9F2E69D98BE CRC64;
MADQYHEPVS ELTGKDRDFV RALNSLKEEI EAVAWYHQRV VTTKDETVRK ILEHNRDEEM
EHAAMLLEWL RRNMPGWDEA LRTYLFTDKP ITEIEEETSG GSENTGGDLG IRKL
