ENCAP_THEP1
ID ENCAP_THEP1 Reviewed; 265 AA.
AC A5IJ00;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Type 1 encapsulin shell protein {ECO:0000250|UniProtKB:Q9WZP2};
DE AltName: Full=Maritimacin;
GN Name=enc {ECO:0000305}; OrderedLocusNames=Tpet_0144;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
CC -!- FUNCTION: Shell component of a type 1 encapsulin nanocompartment.
CC Assembles into proteinaceous shells 23-24 nm in diameter with 2-2.5 nm
CC thick walls. Cargo protein Flp (ferritin-like protein, may store iron)
CC is targeted to the interior via its C-terminal extension.
CC {ECO:0000250|UniProtKB:Q9WZP2}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9WZP2};
CC -!- SUBUNIT: This encapsulin nanocompartment is formed by 60 subunits;
CC monomers form pentamers which assemble to form shells. There are 12
CC pores where the pentamers meet as well as 3-fold axis channels and
CC dimer channels; none are larger than 3-4 Angstroms in diameter. The N-
CC terminus of the protein is inside the shell, the C-terminus is outside.
CC {ECO:0000250|UniProtKB:Q9WZP2}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000250|UniProtKB:Q9WZP2}.
CC -!- SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000702; ABQ46173.1; -; Genomic_DNA.
DR RefSeq; WP_011942839.1; NC_009486.1.
DR AlphaFoldDB; A5IJ00; -.
DR SMR; A5IJ00; -.
DR STRING; 390874.Tpet_0144; -.
DR MEROPS; U56.001; -.
DR EnsemblBacteria; ABQ46173; ABQ46173; Tpet_0144.
DR KEGG; tpt:Tpet_0144; -.
DR eggNOG; COG1659; Bacteria.
DR HOGENOM; CLU_089875_1_0_0; -.
DR OMA; DSDWQPV; -.
DR Proteomes; UP000006558; Chromosome.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR007544; Linocin_M18.
DR Pfam; PF04454; Linocin_M18; 1.
DR PIRSF; PIRSF019254; CFP29; 1.
PE 3: Inferred from homology;
KW Encapsulin nanocompartment; Flavoprotein; FMN; Ion transport; Iron;
KW Iron storage; Iron transport; Transport.
FT CHAIN 1..265
FT /note="Type 1 encapsulin shell protein"
FT /id="PRO_0000343951"
FT REGION 184..189
FT /note="Pore-forming loop"
FT /evidence="ECO:0000250|UniProtKB:Q9WZP2"
FT BINDING 79..81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9WZP2"
FT BINDING 87
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9WZP2"
FT BINDING 235
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9WZP2"
SQ SEQUENCE 265 AA; 30437 MW; C5E4BA88A622B48C CRC64;
MEFLKRSFAP LTEKQWQEID NRAREIFKTQ LYGRKFVDVE GPYGWEYAAH PLGEVEVLSD
ENEVVKWGLR KSLPLIELRA TFTLDLWELD NLERGKPNVD LSSLEETVRK VAEFEDEVIF
RGCEKSGVKG LLSFEERKIE CGSTPKDLLE AIVRALSIFS KDGIEGPYTL VINTDRWVSF
LKEEAGHYPL EKRVEECLRG GKIITTPRIE DALVVSERGG DFKLILGQDL SIGYEDREKD
AVRLFITETF TFQVVNPEAL ILLKF