EUTL_ECOLI
ID EUTL_ECOLI Reviewed; 219 AA.
AC P76541; Q2MAJ1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Bacterial microcompartment shell protein EutL;
DE AltName: Full=BMC-T {ECO:0000305};
DE AltName: Full=Ethanolamine utilization protein EutL;
GN Name=eutL; Synonyms=yffJ; OrderedLocusNames=b2439, JW2432;
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]
RP PRELIMINARY STRUCTURAL CHARACTERIZATION, AND SUBUNIT.
RX PubMed=19194002; DOI=10.1107/s1744309108042127;
RA Nikolakakis K., Ohtaki A., Newton K., Chworos A., Sagermann M.;
RT "Preliminary structural investigations of the Eut-L shell protein of the
RT ethanolamine ammonia-lyase metabolosome of Escherichia coli.";
RL Acta Crystallogr. F 65:128-132(2009).
RN [4] {ECO:0007744|PDB:3GFH}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN CLOSED FORM, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19451619; DOI=10.1073/pnas.0902324106;
RA Sagermann M., Ohtaki A., Nikolakakis K.;
RT "Crystal structure of the EutL shell protein of the ethanolamine ammonia
RT lyase microcompartment.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8883-8887(2009).
RN [5] {ECO:0007744|PDB:3I82, ECO:0007744|PDB:3I87}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN CLOSED AND OPEN FORM, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
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).
RN [6] {ECO:0007744|PDB:3MPV}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC (OPEN FORM),
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20851901; DOI=10.1128/jb.00652-10;
RA Takenoya M., Nikolakakis K., Sagermann M.;
RT "Crystallographic insights into the pore structures and mechanisms of the
RT EutL and EutM shell proteins of the ethanolamine-utilizing microcompartment
RT of Escherichia coli.";
RL J. Bacteriol. 192:6056-6063(2010).
CC -!- FUNCTION: A component of the bacterial microcompartment (BMC) shell
CC dedicated to ethanolamine degradation (Probable). Two crystal forms
CC have been seen; a form with a closed central pore that has 3 very small
CC (1.1-2.2 Angstroms) channels per trimer lined by acidic and aromatic
CC residues (PubMed:19451619, PubMed:20044574). A form with a large
CC central pore (8-12 Angstroms) has also been seen; this is probably a
CC functional pore which allows molecules to enter and exit the BMC in a
CC selective, gated manner (PubMed:20851901, PubMed:20044574). Another
CC group only sees the central pore in the presence of Zn(2+); soaking
CC crystals in ZnCl(2) leads to dramatic conformational changes that open
CC a central pore of about 12 Angstroms. Whether Zn(2+) binding is
CC physiologically relevant is unclear, however it suggests a gating
CC mechanism exists (PubMed:20851901). Ethanolamine-binding by the small
CC channels has been hypothesized to stabilize the EutL central pore in a
CC closed (non-transporting) state. An open pore is thought to be large
CC enough to transport ATP and/or cobalamin (By similarity).
CC {ECO:0000250|UniProtKB:Q8XLZ0, ECO:0000269|PubMed:19451619,
CC ECO:0000269|PubMed:20044574, ECO:0000269|PubMed:20851901,
CC ECO:0000305|PubMed:19451619, ECO:0000305|PubMed:20044574,
CC ECO:0000305|PubMed:20851901, ECO:0007744|PDB:3GFH,
CC ECO:0007744|PDB:3I82, ECO:0007744|PDB:3MPV}.
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer (PubMed:19194002,
CC PubMed:19451619, PubMed:20851901, PubMed:20044574). The trimers form a
CC two-dimensional array about 37 Angstroms thick (PubMed:19451619,
CC PubMed:20044574). {ECO:0000269|PubMed:19194002,
CC ECO:0000269|PubMed:19451619, ECO:0000269|PubMed:20044574,
CC ECO:0000269|PubMed:20851901}.
CC -!- INTERACTION:
CC P76541; P76541: eutL; NbExp=3; IntAct=EBI-1128826, EBI-1128826;
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:19451619, ECO:0000305|PubMed:20044574,
CC ECO:0000305|PubMed:20851901}.
CC -!- DOMAIN: Has 2 BMC domains which can evolve independently of each other.
CC {ECO:0000305|PubMed:19451619}.
CC -!- SIMILARITY: Belongs to the EutL/PduB 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}.
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DR EMBL; U00096; AAC75492.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76715.1; -; Genomic_DNA.
DR PIR; F65018; F65018.
DR RefSeq; NP_416934.1; NC_000913.3.
DR RefSeq; WP_001111023.1; NZ_LN832404.1.
DR PDB; 3GFH; X-ray; 2.20 A; A/B=1-219.
DR PDB; 3I82; X-ray; 2.31 A; A=1-219.
DR PDB; 3I87; X-ray; 2.30 A; A=1-219.
DR PDB; 3MPV; X-ray; 2.60 A; A/B=1-219.
DR PDBsum; 3GFH; -.
DR PDBsum; 3I82; -.
DR PDBsum; 3I87; -.
DR PDBsum; 3MPV; -.
DR AlphaFoldDB; P76541; -.
DR SMR; P76541; -.
DR BioGRID; 4260576; 13.
DR DIP; DIP-9536N; -.
DR IntAct; P76541; 1.
DR STRING; 511145.b2439; -.
DR TCDB; 1.S.2.1.1; the bacterial microcompartment shell/pore-forming protein-2 (bmc-sp2) family.
DR jPOST; P76541; -.
DR PaxDb; P76541; -.
DR PRIDE; P76541; -.
DR EnsemblBacteria; AAC75492; AAC75492; b2439.
DR EnsemblBacteria; BAE76715; BAE76715; BAE76715.
DR GeneID; 946914; -.
DR KEGG; ecj:JW2432; -.
DR KEGG; eco:b2439; -.
DR PATRIC; fig|1411691.4.peg.4292; -.
DR EchoBASE; EB3923; -.
DR eggNOG; COG4816; Bacteria.
DR HOGENOM; CLU_1270774_0_0_6; -.
DR InParanoid; P76541; -.
DR OMA; ACFYSAN; -.
DR PhylomeDB; P76541; -.
DR BioCyc; EcoCyc:G7271-MON; -.
DR UniPathway; UPA00560; -.
DR EvolutionaryTrace; P76541; -.
DR PRO; PR:P76541; -.
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; IPI:IntAct.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.1710; -; 2.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR030983; EutL.
DR InterPro; IPR009193; EutL_PduB.
DR Pfam; PF00936; BMC; 2.
DR PIRSF; PIRSF012290; EutL_PduB; 1.
DR SMART; SM00877; BMC; 2.
DR SUPFAM; SSF143414; SSF143414; 1.
DR TIGRFAMs; TIGR04502; microcomp_EutL; 1.
DR PROSITE; PS51931; BMC_CP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..219
FT /note="Bacterial microcompartment shell protein EutL"
FT /id="PRO_0000201516"
FT DOMAIN 1..113
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 114..215
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT REGION 45..46
FT /note="Part of the acidic patch lining the small pore"
FT /evidence="ECO:0000269|PubMed:19451619"
FT BINDING 45
FT /ligand="ethanolamine"
FT /ligand_id="ChEBI:CHEBI:57603"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT BINDING 46
FT /ligand="ethanolamine"
FT /ligand_id="ChEBI:CHEBI:57603"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT BINDING 83
FT /ligand="ethanolamine"
FT /ligand_id="ChEBI:CHEBI:57603"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT BINDING 113
FT /ligand="ethanolamine"
FT /ligand_id="ChEBI:CHEBI:57603"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3MPV"
FT BINDING 183..185
FT /ligand="ethanolamine"
FT /ligand_id="ChEBI:CHEBI:57603"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT SITE 53
FT /note="Part of the acidic patch lining the small pore"
FT /evidence="ECO:0000269|PubMed:19451619"
FT SITE 70
FT /note="Important for gating"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT SITE 83
FT /note="Part of the acidic patch lining the small pore"
FT /evidence="ECO:0000269|PubMed:19451619"
FT SITE 184
FT /note="Important for gating"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:3GFH"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:3GFH"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3GFH"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3I82"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:3GFH"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3I82"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:3GFH"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:3GFH"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:3GFH"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3GFH"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:3GFH"
SQ SEQUENCE 219 AA; 22788 MW; 1A5417565256243E CRC64;
MPALDLIRPS VTAMRVIASV NADFARELKL PPHIRSLGLI SADSDDVTYI AADEATKQAM
VEVVYGRSLY AGAAHGPSPT AGEVLIMLGG PNPAEVRAGL DAMIAHIENG AAFQWANDAQ
DTAFLAHVVS RTGSYLSSTA GITLGDPMAY LVAPPLEATY GIDAALKSAD VQLATYVPPP
SETNYSAAFL TGSQAACKAA CNAFTDAVLE IARNPIQRA
