ID   EUTS_ECOLI              Reviewed;         111 AA.
AC   P63746; P76557; Q2MAI6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Bacterial microcompartment shell protein EutS;
DE   AltName: Full=Ethanolamine utilization protein EutS;
GN   Name=eutS; Synonyms=ypfE; OrderedLocusNames=b2462, JW2446;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3] {ECO:0007744|PDB:3I96, ECO:0007744|PDB:3IA0}
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, DOMAIN, AND MUTAGENESIS OF GLY-39.
RC   STRAIN=K12;
RX   PubMed=20044574; DOI=10.1126/science.1179513;
RA   Tanaka S., Sawaya M.R., Yeates T.O.;
RT   "Structure and mechanisms of a protein-based organelle in Escherichia
RT   coli.";
RL   Science 327:81-84(2010).
CC   -!- FUNCTION: A component of the bacterial microcompartment (BMC) shell
CC       dedicated to ethanolamine degradation. Its unusual hexameric shape may
CC       help form the BMC shell (Probable). Targets at least 2 proteins (EutC
CC       and EutE) to the interior of the BMC (By similarity). Proteins such as
CC       EutS containing circularly permuted BMC domains may play a key role in
CC       conferring heterogeneity and flexibility in this BMC (Probable).
CC       {ECO:0000250|UniProtKB:Q9ZFV7, ECO:0000305,
CC       ECO:0000305|PubMed:20044574}.
CC   -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC   -!- SUBUNIT: Homohexamer with a central pore; the hexamer is not symmetric,
CC       it is bent by about 40 degrees; bending depends on Gly-39
CC       (PubMed:20044574). Interacts with the N-terminus of EutC and of EutE,
CC       targeting them to the interior of the BMC (By similarity).
CC       {ECO:0000250|UniProtKB:Q9ZFV7, ECO:0000269|PubMed:20044574}.
CC   -!- INTERACTION:
CC       P63746; P63746: eutS; NbExp=2; IntAct=EBI-1128985, EBI-1128985;
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000305|PubMed:20044574}.
CC   -!- DOMAIN: One side of the hexamer is concave and lined by hydrophobic
CC       residues, the other side has a slightly protruding, 6-stranded beta-
CC       barrel. {ECO:0000269|PubMed:20044574}.
CC   -!- SIMILARITY: Belongs to the EutS/PduU family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01279}.
CC   -!- CAUTION: In strain MG1655 the eut operon is interrupted by the CPZ-55
CC       prophage, encoding 9 genes situated between eutA and eutB, which are
CC       translated in the other direction. CPZ-55 may prevent expression of the
CC       eut operon in strain MG1655. Strain W3110 does not have this prophage
CC       element and should be able to express the operon.
CC       {ECO:0000305|PubMed:9278503}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00096; AAC75515.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76720.1; -; Genomic_DNA.
DR   RefSeq; NP_416957.4; NC_000913.3.
DR   RefSeq; WP_000356956.1; NZ_STEB01000051.1.
DR   PDB; 3I96; X-ray; 1.65 A; A/B/C=1-111.
DR   PDB; 3IA0; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v=1-111.
DR   PDBsum; 3I96; -.
DR   PDBsum; 3IA0; -.
DR   AlphaFoldDB; P63746; -.
DR   SMR; P63746; -.
DR   BioGRID; 4260922; 8.
DR   BioGRID; 851275; 1.
DR   IntAct; P63746; 9.
DR   STRING; 511145.b2462; -.
DR   PaxDb; P63746; -.
DR   PRIDE; P63746; -.
DR   EnsemblBacteria; AAC75515; AAC75515; b2462.
DR   EnsemblBacteria; BAE76720; BAE76720; BAE76720.
DR   GeneID; 66673677; -.
DR   GeneID; 946936; -.
DR   KEGG; ecj:JW2446; -.
DR   KEGG; eco:b2462; -.
DR   PATRIC; fig|1411691.4.peg.4278; -.
DR   EchoBASE; EB3944; -.
DR   eggNOG; COG4810; Bacteria.
DR   HOGENOM; CLU_143326_0_0_6; -.
DR   InParanoid; P63746; -.
DR   OMA; AMIAIND; -.
DR   PhylomeDB; P63746; -.
DR   BioCyc; EcoCyc:G7292-MON; -.
DR   UniPathway; UPA00560; -.
DR   EvolutionaryTrace; P63746; -.
DR   PRO; PR:P63746; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc.
DR   CDD; cd07046; BMC_PduU-EutS; 1.
DR   Gene3D; 3.30.70.1710; -; 1.
DR   InterPro; IPR044870; BMC_CP.
DR   InterPro; IPR000249; BMC_dom.
DR   InterPro; IPR037233; CcmK-like_sf.
DR   InterPro; IPR009307; EutS/PduU/CutR.
DR   PANTHER; PTHR40449; PTHR40449; 1.
DR   Pfam; PF00936; BMC; 1.
DR   PIRSF; PIRSF012296; EutS_PduU; 1.
DR   SMART; SM00877; BMC; 1.
DR   SUPFAM; SSF143414; SSF143414; 1.
DR   PROSITE; PS51931; BMC_CP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacterial microcompartment; Reference proteome.
FT   CHAIN           1..111
FT                   /note="Bacterial microcompartment shell protein EutS"
FT                   /id="PRO_0000201520"
FT   DOMAIN          5..103
FT                   /note="BMC circularly permuted"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT   MUTAGEN         39
FT                   /note="G->V: Crystallizes as a symmetric hexamer, migrates
FT                   more slowly in native gels."
FT                   /evidence="ECO:0000269|PubMed:20044574"
FT   STRAND          8..12
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   STRAND          15..23
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   HELIX           27..33
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   STRAND          39..48
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   HELIX           51..62
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   HELIX           83..101
FT                   /evidence="ECO:0007829|PDB:3I96"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:3I96"
SQ   SEQUENCE   111 AA;  11650 MW;  FBA3F8401EAE26C3 CRC64;
     MDKERIIQEF VPGKQVTLAH LIAHPGEELA KKIGVPDAGA IGIMTLTPGE TAMIAGDLAL
     KAADVHIGFL DRFSGALVIY GSVGAVEEAL SQTVSGLGRL LNYTLCEMTK S