EUTL_CLOPE
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 03-AUG-2022, entry version 103.
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; Firmicutes; 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}.
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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 EnsemblBacteria; BAB80606; BAB80606; BAB80606.
DR GeneID; 29571988; -.
DR KEGG; cpe:CPE0900; -.
DR HOGENOM; CLU_1270774_0_0_9; -.
DR OMA; ACFYSAN; -.
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 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; 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
