EUTL_SALTI
ID EUTL_SALTI Reviewed; 219 AA.
AC P0A1D0; Q9ZFU9;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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; OrderedLocusNames=STY2693, t0402;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: A component of the bacterial microcompartment (BMC) shell
CC dedicated to ethanolamine degradation (By similarity). Forms a
CC hexagonal trimer with 3 small channels and a large central pore that
CC has been seen in both open and closed forms and is probably used for
CC gated transport into and out of the BMC (By similarity). Ethanolamine-
CC binding by the small channels has been hypothesized to stabilize the
CC EutL central pore in a closed (non-transporting) state. An open pore is
CC thought to be large enough to transport ATP and/or cobalamin (By
CC similarity). {ECO:0000250|UniProtKB:P0A1C9,
CC ECO:0000250|UniProtKB:P76541, ECO:0000250|UniProtKB:Q8XLZ0}.
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer.
CC {ECO:0000250|UniProtKB:P76541}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:P0A1C9}.
CC -!- DOMAIN: Has 2 BMC domains which can evolve independently of each other.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; AL513382; CAD07687.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68120.1; -; Genomic_DNA.
DR RefSeq; NP_456991.1; NC_003198.1.
DR RefSeq; WP_001111056.1; NZ_WSUR01000025.1.
DR AlphaFoldDB; P0A1D0; -.
DR SMR; P0A1D0; -.
DR STRING; 220341.16503673; -.
DR EnsemblBacteria; AAO68120; AAO68120; t0402.
DR KEGG; stt:t0402; -.
DR KEGG; sty:STY2693; -.
DR PATRIC; fig|220341.7.peg.2730; -.
DR eggNOG; COG4816; Bacteria.
DR HOGENOM; CLU_1270774_0_0_6; -.
DR OMA; ACFYSAN; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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 3: Inferred from homology;
KW Bacterial microcompartment.
FT CHAIN 1..219
FT /note="Bacterial microcompartment shell protein EutL"
FT /id="PRO_0000201517"
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 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 183..185
FT /ligand="ethanolamine"
FT /ligand_id="ChEBI:CHEBI:57603"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT SITE 70
FT /note="Important for gating"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
FT SITE 184
FT /note="Important for gating"
FT /evidence="ECO:0000250|UniProtKB:Q8XLZ0"
SQ SEQUENCE 219 AA; 22696 MW; DA50E6EDF6FCD858 CRC64;
MPALDLIRPS VTAMRVIASV NDGFARELKL PPHIRSLGLI TADSDDVTYI AADEATKQAM
VEVVYGRSLY AGAAHGPSPT AGEVLIMLGG PNPAEVRAGL DAMVASIENG AAFQWANDAE
NTAFLAHVVS RTGSYLSSTA GIALGDPMAY LVAPPLEATF GIDAAMKSAD VQLVTYVPPP
SETNYSAAFL TGSQAACKAA CNAFTDAVLD IARNPVQRA
