ID   ENCAP_RHOE4             Reviewed;         264 AA.
AC   C0ZVK4;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Type 1 encapsulin shell protein {ECO:0000303|PubMed:24981030};
GN   Name=enc {ECO:0000305}; OrderedLocusNames=RER_59900;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   BIOTECHNOLOGY.
RC   STRAIN=N771;
RX   PubMed=24981030; DOI=10.1002/bit.25322;
RA   Tamura A., Fukutani Y., Takami T., Fujii M., Nakaguchi Y., Murakami Y.,
RA   Noguchi K., Yohda M., Odaka M.;
RT   "Packaging guest proteins into the encapsulin nanocompartment from
RT   Rhodococcus erythropolis N771.";
RL   Biotechnol. Bioeng. 112:13-20(2015).
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).
CC   -!- FUNCTION: Shell component of a type 1 encapsulin nanocompartment.
CC       Assembles into proteinaceous shells 21-24 nm in diameter. Empty
CC       organelles can be expressed in E.coli. Cargo proteins (DypB) are
CC       targeted to the interior via their C-terminal extensions.
CC       {ECO:0000269|PubMed:24981030}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Stable as a monodisperse organelle up to 50 degrees Celsius, at
CC         higher temperatures they aggregate. {ECO:0000269|PubMed:24981030};
CC   -!- SUBUNIT: Forms hollow shells composed of 60 subunits (Probable).
CC       Monomers probably form pentamers which assemble into the shell. There
CC       are 12 pores where the pentamers meet as well as 3-fold axis channels
CC       and dimer channels; none are larger than 3-4 Angstroms in diameter. The
CC       N-terminus of the protein is inside the shell, the C-terminus is
CC       outside (By similarity). {ECO:0000250|UniProtKB:Q9WZP2,
CC       ECO:0000305|PubMed:24981030}.
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000269|PubMed:24981030}.
CC   -!- BIOTECHNOLOGY: Foreign proteins can be targeted to ectopic
CC       nanocompartments in E.coli upon coexpression with a construct using the
CC       38 C-terminal residues of DypB (AC C0ZVK5), tested with GFP and
CC       luciferase. Probably only one molecule of each foreign protein is
CC       inside the nanocompartment due to its small interior space.
CC       {ECO:0000269|PubMed:24981030}.
CC   -!- SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP008957; BAH36698.1; -; Genomic_DNA.
DR   RefSeq; WP_020909834.1; NC_012490.1.
DR   SMR; C0ZVK4; -.
DR   STRING; 234621.RER_59900; -.
DR   MEROPS; U56.001; -.
DR   EnsemblBacteria; BAH36698; BAH36698; RER_59900.
DR   KEGG; rer:RER_59900; -.
DR   PATRIC; fig|234621.6.peg.6580; -.
DR   eggNOG; COG1659; Bacteria.
DR   HOGENOM; CLU_089875_1_0_11; -.
DR   OMA; DSDWQPV; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR   InterPro; IPR007544; Linocin_M18.
DR   Pfam; PF04454; Linocin_M18; 1.
DR   PIRSF; PIRSF019254; CFP29; 1.
PE   1: Evidence at protein level;
KW   Encapsulin nanocompartment.
FT   CHAIN           1..264
FT                   /note="Type 1 encapsulin shell protein"
FT                   /id="PRO_0000455317"
SQ   SEQUENCE   264 AA;  28671 MW;  12885FBC86706ED3 CRC64;
     MTNLHRDLAP ISAAAWAEIE EEASRTFKRH VAGRRVVDVE GPSGDDLAAI PLGHQVPINP
     LADGVIAHAR QSQPVIELRV PFTVSRQAID DVERGAKDSD WQPVKDAAKQ IAFAEDRAIF
     EGYPAASITG VRASGSNPEL KLPIDAKDYP EAISQAITSL RLAGVNGPYS LLLNADAFTA
     INETSDHGYP IREHLRRVLD GEIIWAPAID GAFLLSTRGG DYELHLGQDL SIGYLSHDAN
     SVELYFQESM TFLMYTSEAV VSLA