ID EUTL_CLOPE Reviewed; 217 AA. AC Q8XLZ0; DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Bacterial microcompartment shell protein EutL; DE AltName: Full=BMC-T {ECO:0000305}; DE AltName: Full=Ethanolamine utilization protein EutL; DE AltName: Full=EutL microcompartment shell protein {ECO:0000303|PubMed:25752492}; GN Name=eutL; OrderedLocusNames=CPE0900; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh- RT eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). RN [2] {ECO:0007744|PDB:4U6I} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH COBALAMIN IN CLOSED RP FORM, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=13 / Type A; RX PubMed=25484204; DOI=10.1107/s2053230x1402158x; RA Thompson M.C., Crowley C.S., Kopstein J., Bobik T.A., Yeates T.O.; RT "Structure of a bacterial microcompartment shell protein bound to a RT cobalamin cofactor."; RL Acta Crystallogr. F Struct. Biol. Commun. 70:1584-1590(2014). RN [3] {ECO:0007744|PDB:4EDI, ECO:0007744|PDB:4FDZ, ECO:0007744|PDB:4TM6, ECO:0007744|PDB:4TME} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN CLOSED FORM; NATIVE AND REDUCED RP FORMS; IN COMPLEX WITH ETHANOLAMINE, FUNCTION, ETHANOLAMINE-BINDING, RP SUBUNIT, SUBCELLULAR LOCATION, AND DISULFIDE BONDS. RC STRAIN=13 / Type A; RX PubMed=25752492; DOI=10.1002/pro.2672; RA Thompson M.C., Cascio D., Leibly D.J., Yeates T.O.; RT "An allosteric model for control of pore opening by substrate binding in RT the EutL microcompartment shell protein."; RL Protein Sci. 24:956-975(2015). RN [4] {ECO:0007744|PDB:4TLH, ECO:0007744|PDB:6ARC, ECO:0007744|PDB:6ARD} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, SUBUNIT, AND SUBCELLULAR RP LOCATION. RC STRAIN=13 / Type A; RX PubMed=29717712; DOI=10.1107/s2059798318003479; RA Thompson M.C., Cascio D., Yeates T.O.; RT "Microfocus diffraction from different regions of a protein crystal: RT structural variations and unit-cell polymorphism."; RL Acta Crystallogr. D 74:411-421(2018). CC -!- FUNCTION: A component of the bacterial microcompartment (BMC) shell CC dedicated to ethanolamine degradation. May be involved in cofactor CC diffusion across the BMC (Probable). Cobalamin is covalently bound to 1 CC subunit of the trimer on the concave (lumenal) face in a closed pore CC conformation; whether this is physiologically relevant is unclear CC (PubMed:25484204). The closed form has 3 very narrow channels (1.3 CC Angstrom at their narrowest) per trimer lined by acidic and aromatic CC residues; 2 ethanolamine molecules can bind in each channel, on either CC side of the constriction. Does not bind acetate, ethanol or acetyl CC phosphate, all of which are small molecules involved in ethanolamine CC metabolism (PubMed:25752492). Ethanolamine-binding has been CC hypothesized to stabilize the EutL central pore in a closed (non- CC transporting) state. An open pore is thought to be large enough to CC transport ATP and/or cobalamin (Probable). CC {ECO:0000269|PubMed:25484204, ECO:0000269|PubMed:25752492, CC ECO:0000305|PubMed:25484204, ECO:0000305|PubMed:25752492, CC ECO:0000305|PubMed:29717712}. CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer. CC {ECO:0000269|PubMed:25484204, ECO:0000269|PubMed:25752492, CC ECO:0000269|PubMed:29717712}. CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment CC {ECO:0000305|PubMed:25484204, ECO:0000305|PubMed:25752492, CC ECO:0000305|PubMed:29717712}. CC -!- DOMAIN: Has 2 BMC domains which can evolve independently of each other CC (Probable). Two ethanolamine molecules bind in the interface between CC these 2 domains. Ethanolamine 1 binds on the cytoplasmic side, while CC ethanolamine 2 binds on the lumenal side of the BMC (PubMed:25752492). CC {ECO:0000269|PubMed:25752492, ECO:0000305}. CC -!- PTM: A disulfide bond is seen in native crystals; it disappears upon CC reduction with tris-(2-carboxyethyl) phosphine, which also reduces the CC protein's affinity for ethanolamine. It has been suggested to confer CC redox modulation to pore opening. {ECO:0000269|PubMed:25752492, CC ECO:0007744|PDB:4EDI, ECO:0007744|PDB:4FDZ}. CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE- CC ProRule:PRU01279}. 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; BA000016; BAB80606.1; -; Genomic_DNA. DR RefSeq; WP_003461990.1; NC_003366.1. DR PDB; 4EDI; X-ray; 2.00 A; A/B/C=1-217. DR PDB; 4FDZ; X-ray; 1.80 A; A/B/C=1-217. DR PDB; 4TLH; X-ray; 1.70 A; A/B/C=1-217. DR PDB; 4TM6; X-ray; 1.90 A; A/B/C=1-217. DR PDB; 4TME; X-ray; 1.70 A; A/B/C=1-217. DR PDB; 4U6I; X-ray; 2.10 A; A/B/C=1-217. DR PDB; 6ARC; X-ray; 1.90 A; A/B/C=1-217. DR PDB; 6ARD; X-ray; 2.00 A; A/B/C=1-217. DR PDBsum; 4EDI; -. DR PDBsum; 4FDZ; -. DR PDBsum; 4TLH; -. DR PDBsum; 4TM6; -. DR PDBsum; 4TME; -. DR PDBsum; 4U6I; -. DR PDBsum; 6ARC; -. DR PDBsum; 6ARD; -. DR AlphaFoldDB; Q8XLZ0; -. DR SMR; Q8XLZ0; -. DR STRING; 195102.gene:10490163; -. DR GeneID; 69448654; -. DR KEGG; cpe:CPE0900; -. DR HOGENOM; CLU_1270774_0_0_9; -. DR Proteomes; UP000000818; Chromosome. DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR CDD; cd07049; BMC_EutL_repeat1; 1. DR CDD; cd07050; BMC_EutL_repeat2; 1. 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 NCBIfam; TIGR04502; microcomp_EutL; 1. DR Pfam; PF00936; BMC; 2. DR PIRSF; PIRSF012290; EutL_PduB; 1. DR SMART; SM00877; BMC; 2. DR SUPFAM; SSF143414; CcmK-like; 1. DR PROSITE; PS51931; BMC_CP; 2. PE 1: Evidence at protein level; KW 3D-structure; Bacterial microcompartment; Cobalamin; Cobalt; KW Disulfide bond; Metal-binding; Reference proteome. FT CHAIN 1..217 FT /note="Bacterial microcompartment shell protein EutL" FT /id="PRO_0000452913" FT DOMAIN 1..110 FT /note="BMC circularly permuted 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279" FT DOMAIN 111..217 FT /note="BMC circularly permuted 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279" FT BINDING 32 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /ligand_part="Co" FT /ligand_part_id="ChEBI:CHEBI:27638" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:25484204, FT ECO:0007744|PDB:4U6I" FT BINDING 44 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4TME" FT BINDING 45 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4TME" FT BINDING 82 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4TME" FT BINDING 112 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4TME" FT BINDING 176 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4TME" FT BINDING 180 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4TME" FT BINDING 182..184 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:4TME" FT BINDING 184 FT /ligand="ethanolamine" FT /ligand_id="ChEBI:CHEBI:57603" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4TME" FT SITE 69 FT /note="Important for gating" FT /evidence="ECO:0000305|PubMed:25752492" FT SITE 74 FT /note="Important for gating" FT /evidence="ECO:0000305|PubMed:25752492" FT SITE 183 FT /note="Important for gating" FT /evidence="ECO:0000305|PubMed:25752492" FT DISULFID 127..200 FT /evidence="ECO:0000269|PubMed:25752492, FT ECO:0007744|PDB:4EDI" FT STRAND 10..18 FT /evidence="ECO:0007829|PDB:4TLH" FT HELIX 21..26 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:4TLH" FT HELIX 44..57 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:4TLH" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:4TLH" FT TURN 78..82 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 83..91 FT /evidence="ECO:0007829|PDB:4TLH" FT HELIX 92..106 FT /evidence="ECO:0007829|PDB:4TLH" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 121..130 FT /evidence="ECO:0007829|PDB:4TLH" FT HELIX 133..139 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 146..152 FT /evidence="ECO:0007829|PDB:4TLH" FT HELIX 154..167 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:4TLH" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:4TLH" FT HELIX 193..211 FT /evidence="ECO:0007829|PDB:4TLH" SQ SEQUENCE 217 AA; 22629 MW; AC934D3655273311 CRC64; MKNDLIRPNV LSVKIISNVS PEMAKKLELE PHHKSLGLIT ADCDDVTYTA LDEATKAAEV DVVYARSMYA GAGNASTKLA GEVIGILAGP SPAEVRSGLN ATLDFIDSGV GFVSANEDDS ICYYAQCVSR TGSYLSKTAG IREGEALAYL VAPPLEAMYA LDAALKAADV EMCEFFAPPT ETNFAGALLT GSQSACKAAC DAFAEAVQSV ASNPLGF //