ENCP1_PYRFU
ID ENCP1_PYRFU Reviewed; 345 AA.
AC Q8U1L4; Q401P1; Q8U1L5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ferritin-like-encapsulin shell fusion protein;
DE AltName: Full=Type 1 encapsulin shell protein;
DE AltName: Full=Virus-like particle {ECO:0000303|PubMed:16091594};
GN Name=enc {ECO:0000305};
GN OrderedLocusNames=PF1192/PF1191 {ECO:0000305|PubMed:16091594};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9; 53-84; 92-132;
RP 160-169 AND 171-216, SEQUENCE REVISION TO 91, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=16091594; DOI=10.1093/jb/mvi111;
RA Namba K., Hagiwara K., Tanaka H., Nakaishi Y., Chong K.T., Yamashita E.,
RA Armah G.E., Ono Y., Ishino Y., Omura T., Tsukihara T., Nakagawa A.;
RT "Expression and molecular characterization of spherical particles derived
RT from the genome of the hyperthermophilic euryarchaeote Pyrococcus
RT furiosus.";
RL J. Biochem. 138:193-199(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP CLASSIFICATION.
RX PubMed=34362927; DOI=10.1038/s41467-021-25071-y;
RA Andreas M.P., Giessen T.W.;
RT "Large-scale computational discovery and analysis of virus-derived
RT microbial nanocompartments.";
RL Nat. Commun. 12:4748-4748(2021).
RN [4] {ECO:0007744|PDB:2E0Z}
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=17397865; DOI=10.1016/j.jmb.2007.02.075;
RA Akita F., Chong K.T., Tanaka H., Yamashita E., Miyazaki N., Nakaishi Y.,
RA Suzuki M., Namba K., Ono Y., Tsukihara T., Nakagawa A.;
RT "The crystal structure of a virus-like particle from the hyperthermophilic
RT archaeon Pyrococcus furiosus provides insight into the evolution of
RT viruses.";
RL J. Mol. Biol. 368:1469-1483(2007).
CC -!- FUNCTION: Fusion of the shell and cargo protein of a type 1 encapsulin
CC nanocompartment (PubMed:17397865). The nanocompartment is probably
CC involved in iron storage (Probable). Expression in E.coli generates
CC spherical particles (PfSPs) about 30 nm in diameter (PubMed:16091594).
CC {ECO:0000269|PubMed:16091594, ECO:0000269|PubMed:17397865,
CC ECO:0000305}.
CC -!- SUBUNIT: 180 monomers assemble into 12 pentamers and 20 hexamers which
CC further assemble into an icosahedral particle about 36.6 nm in
CC diameter. {ECO:0000269|PubMed:17397865}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:16091594, ECO:0000269|PubMed:17397865}.
CC -!- DOMAIN: The ferritin-like domain N-terminal 109 disordered residues are
CC located inside the organelle in the crystal. The rest of the protein
CC has 3 structural domains; a discontinuous peripheral domain (P, 110-
CC 138, 167-210, 304-334), an elongated loop (E, 139-166) and the
CC discontinuous axial domain (A, 211-303 and 335-345). The E loop is
CC highly flexible and allows formation of the pentamers and hexamers from
CC the same protein. {ECO:0000269|PubMed:17397865}.
CC -!- MISCELLANEOUS: Shows substantial structural similarity to gp5 of the
CC HK97 viral capsid, and while the sequence homology is weak, it suggests
CC this protein may have evolved from a viral capsid protein.
CC {ECO:0000305|PubMed:17397865}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ferritin-like
CC superfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the encapsulin
CC family. Family 1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL81315.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL81316.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB214633; BAE19947.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81316.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE009950; AAL81315.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; WP_014835352.1; NC_018092.1.
DR PDB; 2E0Z; X-ray; 3.60 A; A/B/C=1-345.
DR PDBsum; 2E0Z; -.
DR STRING; 186497.PF1192; -.
DR DNASU; 1469062; -.
DR EnsemblBacteria; AAL81315; AAL81315; PF1191.
DR EnsemblBacteria; AAL81316; AAL81316; PF1192.
DR GeneID; 41713000; -.
DR KEGG; pfu:PF1191; -.
DR KEGG; pfu:PF1192; -.
DR PATRIC; fig|186497.12.peg.1253; -.
DR eggNOG; arCOG03349; Archaea.
DR HOGENOM; CLU_141525_1_0_2; -.
DR OMA; MPEFANP; -.
DR PhylomeDB; Q8U1L4; -.
DR EvolutionaryTrace; Q8U1L4; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR007544; Linocin_M18.
DR InterPro; IPR003251; Rubrerythrin.
DR Pfam; PF04454; Linocin_M18; 1.
DR Pfam; PF02915; Rubrerythrin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Encapsulin nanocompartment;
KW Ion transport; Iron; Iron storage; Iron transport; Metal-binding;
KW Reference proteome; Transport.
FT CHAIN 1..345
FT /note="Ferritin-like-encapsulin shell fusion protein"
FT /id="PRO_0000455319"
FT REGION 1..109
FT /note="Ferritin-like domain"
FT /evidence="ECO:0000305|PubMed:17397865"
FT REGION 110..345
FT /note="Encapsulin domain"
FT /evidence="ECO:0000305|PubMed:17397865"
FT BINDING 31
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 31
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2RVS1"
SQ SEQUENCE 345 AA; 38802 MW; 1A05C20EA8EA8A03 CRC64;
MLSINPTLIN RDKPYTKEEL MEILRLAIIA ELDAINLYEQ MARYSEDENV RKILLDVARE
EKAHVGEFMA LLLNLDPEQV TELKGGFEEV KELTGIEAHI NDNKKEESNV EYFEKLRSAL
LDGVNKGRSL LKHLPVTRIE GQSFRVDIIK FEDGVRVVKQ EYKPIPLLKK KFYVGIRELN
DGTYDVSIAT KAGELLVKDE ESLVIREILS TEGIKKMKLS SWDNPEEALN DLMNALQEAS
NASAGPFGLI INPKRYAKLL KIYEKSGKML VEVLKEIFRG GIIVTLNIDE NKVIIFANTP
AVLDVVVGQD VTLQELGPEG DDVAFLVSEA IGIRIKNPEA IVVLE
