ID   ENCAP_MYXXD             Reviewed;         287 AA.
AC   Q1D6H4;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Type 1 encapsulin shell protein EncA {ECO:0000303|PubMed:25024436};
GN   Name=encA {ECO:0000303|PubMed:25024436}; ORFNames=MXAN_3556;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN   [2]
RP   OPERON STRUCTURE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DZ2;
RX   PubMed=19996678; DOI=10.4014/jmb.0903.0112;
RA   Kim D., Chung J., Hyun H., Lee C., Lee K., Cho K.;
RT   "Operon required for fruiting body development in Myxococcus xanthus.";
RL   J. Microbiol. Biotechnol. 19:1288-1294(2009).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC   STRAIN=DK1622;
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:4PT2}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.60 ANGSTROMS) OF 1-287, IDENTIFICATION
RP   BY MASS SPECTROMETRY, SEQUENCE REVISION TO N-TERMINUS, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, INDUCTION BY STARVATION, DOMAIN, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=DK1622;
RX   PubMed=25024436; DOI=10.15252/embj.201488566;
RA   McHugh C.A., Fontana J., Nemecek D., Cheng N., Aksyuk A.A., Heymann J.B.,
RA   Winkler D.C., Lam A.S., Wall J.S., Steven A.C., Hoiczyk E.;
RT   "A virus capsid-like nanocompartment that stores iron and protects bacteria
RT   from oxidative stress.";
RL   EMBO J. 33:1896-1911(2014).
CC   -!- FUNCTION: Shell component of a type 1, iron-storage encapsulin
CC       nanocompartment. Encapsulin nanocompartments are 32 nm in diameter with
CC       an iron- and phosphorus-rich core (4Fe:1P) about 24 nm in diameter.
CC       Upon expression in E.coli most particles are 32 nm, 20% are 18 nm. The
CC       core is filled with an average of 14 dense granules, 5-6 nm in diameter
CC       that are not evenly distributed. Each nanocompartment is estimated to
CC       hold 30,000-35,000 Fe atoms (PubMed:25024436, PubMed:31194509). The
CC       minor proteins EncB, EncC and EncD probably lie against the interior
CC       face of the nanocompartment (Probable). {ECO:0000269|PubMed:25024436,
CC       ECO:0000269|PubMed:31194509, ECO:0000305|PubMed:25024436}.
CC   -!- SUBUNIT: The 32 nm encapsulin nanocompartment is formed by 180
CC       subunits; monomers form pentamers which assemble to form shells. There
CC       are 36 pores where the pentamers meet as well as 3-fold axis channels
CC       and dimer channels. The N-terminus of the protein is inside the shell.
CC       {ECO:0000269|PubMed:25024436}.
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000269|PubMed:25024436, ECO:0000269|PubMed:31194509}.
CC   -!- INDUCTION: Part of the MXAN_3553-MXAN_3554-MXAN_3555-encA operon
CC       (PubMed:19996678). Expression is induced by amino acid starvation (at
CC       protein level). Not present in spores (at protein level)
CC       (PubMed:25024436). {ECO:0000269|PubMed:19996678,
CC       ECO:0000269|PubMed:25024436}.
CC   -!- DOMAIN: Has 3 domains; a discontinuous peripheral domain (P), an
CC       elongated loop (E) and the discontinuous axial domain (A).
CC       {ECO:0000269|PubMed:25024436}.
CC   -!- DISRUPTION PHENOTYPE: Does not form fruiting bodies (PubMed:19996678).
CC       Decreased survival when grown under oxidative stress (0.5 mM H2O2)
CC       (PubMed:25024436). {ECO:0000269|PubMed:19996678,
CC       ECO:0000269|PubMed:25024436}.
CC   -!- BIOTECHNOLOGY: The encapsulin and a cargo construct (an encB-encC-encD
CC       fusion) can be overexpressed in E.coli and in human HEK293T cells. In
CC       HEK293T in the presence of 0.5 M ferrous ammonium sulfate
CC       nanocompartments can be detected and used as cell markers. Coexpression
CC       of this nanocompartment with a larger nanocompartment from
CC       Q.thermotolerans (AC A0A0F5HPP7) allows expression of different sized
CC       iron-rich particles. The encapsulin shell proteins do not seem to mix.
CC       {ECO:0000269|PubMed:31194509}.
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:25024436}.
CC   -!- SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF87797.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000269|PubMed:25024436};
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DR   EMBL; CP000113; ABF87797.1; ALT_INIT; Genomic_DNA.
DR   PDB; 4PT2; EM; 4.60 A; A/B/P=1-287.
DR   PDB; 7S20; EM; 3.40 A; A/B/C=1-287.
DR   PDB; 7S21; EM; 3.40 A; A=1-287.
DR   PDB; 7S2T; EM; 3.45 A; A/B/C=1-287.
DR   PDB; 7S4Q; EM; 3.12 A; A/B/C=1-287.
DR   PDBsum; 4PT2; -.
DR   PDBsum; 7S20; -.
DR   PDBsum; 7S21; -.
DR   PDBsum; 7S2T; -.
DR   PDBsum; 7S4Q; -.
DR   SMR; Q1D6H4; -.
DR   IntAct; Q1D6H4; 1.
DR   MINT; Q1D6H4; -.
DR   STRING; 246197.MXAN_3556; -.
DR   EnsemblBacteria; ABF87797; ABF87797; MXAN_3556.
DR   KEGG; mxa:MXAN_3556; -.
DR   eggNOG; COG1659; Bacteria.
DR   HOGENOM; CLU_089875_0_0_7; -.
DR   OMA; DSDWQPV; -.
DR   BRENDA; 1.16.3.1; 3551.
DR   Proteomes; UP000002402; Chromosome.
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.
DR   PIRSF; PIRSF019254; CFP29; 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..287
FT                   /note="Type 1 encapsulin shell protein EncA"
FT                   /id="PRO_0000455315"
SQ   SEQUENCE   287 AA;  31656 MW;  5F3BDD27DB2B55E4 CRC64;
     MPDFLGHAEN PLREEEWARL NETVIQVARR SLVGRRILDI YGPLGAGVQT VPYDEFQGVS
     PGAVDIVGEQ ETAMVFTDAR KFKTIPIIYK DFLLHWRDIE AARTHNMPLD VSAAAGAAAL
     CAQQEDELIF YGDARLGYEG LMTANGRLTV PLGDWTSPGG GFQAIVEATR KLNEQGHFGP
     YAVVLSPRLY SQLHRIYEKT GVLEIETIRQ LASDGVYQSN RLRGESGVVV STGRENMDLA
     VSMDMVAAYL GASRMNHPFR VLEALLLRIK HPDAICTLEG AGATERR