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 24-JAN-2024, entry version 108. 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; Pseudomonadota; 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}. 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; 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; 511145-b2457; -. DR EnsemblBacteria; AAC75510; AAC75510; b2457. DR GeneID; 83579987; -. 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 OrthoDB; 9812608at2; -. DR PhylomeDB; P0ABF4; -. DR BioCyc; EcoCyc:G7287-MONOMER; -. DR UniPathway; UPA00560; -. DR EvolutionaryTrace; P0ABF4; -. DR PRO; PR:P0ABF4; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; ISS:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0005198; F:structural molecule activity; ISS:EcoCyc. DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc. DR CDD; cd07045; BMC_CcmK_like; 1. 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 PANTHER; PTHR33941:SF10; BACTERIAL MICROCOMPARTMENT SHELL PROTEIN EUTM; 1. DR PANTHER; PTHR33941; PROPANEDIOL UTILIZATION PROTEIN PDUA; 1. DR Pfam; PF00936; BMC; 1. DR SMART; SM00877; BMC; 1. DR SUPFAM; SSF143414; CcmK-like; 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 //