EUTM_ECOLI
ID EUTM_ECOLI Reviewed; 97 AA.
AC P0ABF4; P77606;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Bacterial microcompartment shell protein EutM;
DE AltName: Full=Bacterial microcompartment protein homohexamer {ECO:0000305};
DE Short=BMC-H {ECO:0000305};
DE AltName: Full=Ethanolamine utilization protein EutM;
GN Name=eutM; Synonyms=cchA, yffZ; OrderedLocusNames=b2457, JW2441;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
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 [3]
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 [4] {ECO:0007744|PDB:3MPW, ECO:0007744|PDB:3MPY}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, AND SUBUNIT.
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).
RN [5] {ECO:0007744|PDB:3I6P}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), FUNCTION, AND SUBUNIT.
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: Probably a major component of the bacterial microcompartment
CC (BMC) shell dedicated to ethanolamine degradation (Probable). Each
CC homohexamer has a central pore with an opening of up to 8.6 Angstroms.
CC A positively-charged funnel leads to the pore from each side of the
CC hexamer; a phosphate or sulfate ion is found in the pore. The pore
CC probably allows metabolite passage into and out of the BMC
CC (PubMed:20851901, PubMed:20044574). {ECO:0000269|PubMed:20044574,
CC ECO:0000269|PubMed:20851901, ECO:0000305|PubMed:20044574,
CC ECO:0000305|PubMed:20851901}.
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC -!- SUBUNIT: Homohexamer with a central pore of up to 8.6 Angstroms
CC diameter. The hexamers pack into a two-dimensional array
CC (PubMed:20851901, PubMed:20044574). Interacts with EutQ (By
CC similarity). {ECO:0000250|UniProtKB:P41791,
CC ECO:0000269|PubMed:20044574, ECO:0000269|PubMed:20851901}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:P41791}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278}.
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; AAC75510.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16335.2; -; Genomic_DNA.
DR RefSeq; NP_416952.2; NC_000913.3.
DR RefSeq; WP_000387713.1; NZ_STEB01000051.1.
DR PDB; 3I6P; X-ray; 2.10 A; A/B/C/D/E/F=1-97.
DR PDB; 3MPW; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-97.
DR PDB; 3MPY; X-ray; 2.00 A; A=1-97.
DR PDBsum; 3I6P; -.
DR PDBsum; 3MPW; -.
DR PDBsum; 3MPY; -.
DR AlphaFoldDB; P0ABF4; -.
DR SMR; P0ABF4; -.
DR BioGRID; 4260926; 10.
DR DIP; DIP-9537N; -.
DR IntAct; P0ABF4; 2.
DR STRING; 511145.b2457; -.
DR TCDB; 1.S.1.1.2; the bacterial microcompartment shell/pore-forming protein-1 (bmc-sp1) family.
DR PaxDb; P0ABF4; -.
DR PRIDE; P0ABF4; -.
DR EnsemblBacteria; AAC75510; AAC75510; b2457.
DR EnsemblBacteria; BAA16335; BAA16335; BAA16335.
DR GeneID; 67416845; -.
DR GeneID; 946942; -.
DR KEGG; ecj:JW2441; -.
DR KEGG; eco:b2457; -.
DR PATRIC; fig|511145.12.peg.2551; -.
DR EchoBASE; EB3939; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_3_6; -.
DR InParanoid; P0ABF4; -.
DR OMA; QFREGVN; -.
DR PhylomeDB; P0ABF4; -.
DR BioCyc; EcoCyc:G7287-MON; -.
DR UniPathway; UPA00560; -.
DR EvolutionaryTrace; P0ABF4; -.
DR PRO; PR:P0ABF4; -.
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 Gene3D; 3.30.70.1710; -; 1.
DR InterPro; IPR020808; Bact_microcomp_CS.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR Pfam; PF00936; BMC; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS01139; BMC_1; 1.
DR PROSITE; PS51930; BMC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Reference proteome.
FT CHAIN 1..97
FT /note="Bacterial microcompartment shell protein EutM"
FT /id="PRO_0000004786"
FT DOMAIN 3..87
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:3MPY"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:3MPY"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:3MPY"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:3MPY"
FT HELIX 49..66
FT /evidence="ECO:0007829|PDB:3MPY"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:3MPY"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:3MPY"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3MPY"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:3MPW"
SQ SEQUENCE 97 AA; 9866 MW; 0A4170FD8ABB8CF8 CRC64;
MEALGMIETR GLVALIEASD AMVKAARVKL VGVKQIGGGL CTAMVRGDVA ACKAATDAGA
AAAQRIGELV SVHVIPRPHG DLEEVFPIGL KGDSSNL
