ENCAP_QUATH
ID ENCAP_QUATH Reviewed; 282 AA.
AC A0A0F5HPP7; A0A0F5IDU5;
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=Type 1 encapsulin shell protein;
DE AltName: Full=IMEF encapsulin {ECO:0000303|PubMed:28263314};
GN Name=enc {ECO:0000303|PubMed:28263314}; ORFNames=QY95_01592;
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, AND SUBCELLULAR LOCATION.
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, SUBUNIT, SUBCELLULAR LOCATION, AND 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]
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 [5] {ECO:0007744|PDB:6NJ8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.85 ANGSTROMS), FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
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: Shell component of a type 1 encapsulin nanocompartment.
CC Assembles into proteinaceous icosahedral shells 42-43 nm in diameter
CC with an iron- and phosphorus-rich core (1Fe:1.1P) which can store over
CC 23,000-35,000 iron atoms (with a calculated maximum of 83,000 Fe).
CC There are 2 types of negatively charged open pores in the cryo-electron
CC structure; a 3-fold pore where 3 hexamers meet with a minimal size of
CC 7.2 Angstroms and a 5-fold pore where pentamers meet with a minimal
CC size of 2.3 Angstroms. The 2-fold pore seen in other encapsulin
CC nanocompartments is closed. Empty compartments can be generated in
CC E.coli (PubMed:28263314, PubMed:31282860, PubMed:31194509). Both types
CC of pore have extra density in their centers in the structure
CC (PubMed:31282860). 2 different cargo proteins have been identified
CC (IMEF and Fer); when both are expressed in E.coli with the shell
CC protein only IMEF is detected within the nanocompartment. E.coli
CC expressing all 3 genes stores the largest amount of iron and is
CC protected from Fe/H2O2-induced oxidative stress (PubMed:28263314). Part
CC of the iron-mineralizing encapsulin-associated Firmicute (IMEF) system
CC (Probable). {ECO:0000269|PubMed:28263314, ECO:0000269|PubMed:31194509,
CC ECO:0000269|PubMed:31282860, ECO:0000305|PubMed:28263314}.
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: Initially thought to form a 180 subunit shell
CC (PubMed:28263314). Forms hollow shells composed of 240 subunits, making
CC a shell about 42-43 nm in diameter (PubMed:31282860, PubMed:31194509).
CC The monomer is capable of assuming 4 different conformations which
CC allows packaging into the icosahedron. The shell has 12 pentameric and
CC 30 hexameric capsomers which form the vertices and faces of the
CC icosahedral nanocompartment (PubMed:31282860).
CC {ECO:0000269|PubMed:28263314, ECO:0000269|PubMed:31194509,
CC ECO:0000269|PubMed:31282860}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:31194509, ECO:0000269|PubMed:31282860}.
CC -!- DOMAIN: Formed of E- and discontuous A- and P-loops. A-loops form the
CC main pores while A- and E-loops are the most flexible parts. E- and P-
CC loops of neighboring monomers arrange head-to-tail and form a chainmail
CC topology. {ECO:0000269|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 do not seem to mix.
CC {ECO:0000269|PubMed:31194509}.
CC -!- SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; JWIR02000003; KKB43347.1; -; Genomic_DNA.
DR RefSeq; WP_039238471.1; NZ_JWJE02000035.1.
DR PDB; 6NJ8; EM; 3.85 A; A/B/C/D=1-282.
DR PDB; 7MH2; EM; 3.57 A; A/B/C/D=1-282.
DR PDBsum; 6NJ8; -.
DR PDBsum; 7MH2; -.
DR SMR; A0A0F5HPP7; -.
DR STRING; 1221996.QY95_01592; -.
DR EnsemblBacteria; KKB43347; KKB43347; QY95_01592.
DR OrthoDB; 1252793at2; -.
DR Proteomes; UP000031563; Unassembled WGS sequence.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Encapsulin nanocompartment; Ion transport; Iron;
KW Iron storage; Iron transport; Reference proteome; Transport.
FT CHAIN 1..282
FT /note="Type 1 encapsulin shell protein"
FT /id="PRO_0000455316"
FT SITE 9
FT /note="3-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:31282860"
FT SITE 71
FT /note="3-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:31282860"
FT SITE 200
FT /note="5-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:31282860"
FT SITE 251
FT /note="3-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:31282860"
FT SITE 252
FT /note="3-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:31282860"
SQ SEQUENCE 282 AA; 32204 MW; 51319738AD7F818A CRC64;
MNKSQLYPDS PLTDQDFNQL DQTVIEAARR QLVGRRFIEL YGPLGRGMQS VFNDIFMESH
EAKMDFQGSF DTEVESSRRV NYTIPMLYKD FVLYWRDLEQ SKALDIPIDF SVAANAARDV
AFLEDQMIFH GSKEFDIPGL MNVKGRLTHL IGNWYESGNA FQDIVEARNK LLEMNHNGPY
ALVLSPELYS LLHRVHKDTN VLEIEHVREL ITAGVFQSPV LKGKSGVIVN TGRNNLDLAI
SEDFETAYLG EEGMNHPFRV YETVVLRIKR PAAICTLIDP EE
