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   27-MAR-2024, entry version 92.
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; Pseudomonadota; 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.gene:17586591; -.
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; HCISRTG; -.
DR   OrthoDB; 3283at2; -.
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   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   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
//