ID   EUTL_SALTY              Reviewed;         219 AA.
AC   P0A1C9; Q9ZFU9;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=STM2456;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=10464203; DOI=10.1128/jb.181.17.5317-5329.1999;
RA   Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT   "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes
RT   five homologues of carboxysome shell proteins.";
RL   J. Bacteriol. 181:5317-5329(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   FUNCTION, PATHWAY, OPERON, AND INDUCTION BY ETHANOLAMINE AND COBALAMIN.
RC   STRAIN=LT2;
RX   PubMed=3045078; DOI=10.1128/jb.170.9.3855-3863.1988;
RA   Roof D.M., Roth J.R.;
RT   "Ethanolamine utilization in Salmonella typhimurium.";
RL   J. Bacteriol. 170:3855-3863(1988).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=16291677; DOI=10.1128/jb.187.23.8039-8046.2005;
RA   Brinsmade S.R., Paldon T., Escalante-Semerena J.C.;
RT   "Minimal functions and physiological conditions required for growth of
RT   salmonella enterica on ethanolamine in the absence of the metabolosome.";
RL   J. Bacteriol. 187:8039-8046(2005).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA   Penrod J.T., Roth J.R.;
RT   "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT   in Salmonella enterica.";
RL   J. Bacteriol. 188:2865-2874(2006).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC   STRAIN=LT2;
RX   PubMed=22428024; DOI=10.1371/journal.pone.0033342;
RA   Choudhary S., Quin M.B., Sanders M.A., Johnson E.T., Schmidt-Dannert C.;
RT   "Engineered protein nano-compartments for targeted enzyme localization.";
RL   PLoS ONE 7:e33342-e33342(2012).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=23585538; DOI=10.1128/jb.02179-12;
RA   Huseby D.L., Roth J.R.;
RT   "Evidence that a metabolic microcompartment contains and recycles private
RT   cofactor pools.";
RL   J. Bacteriol. 195:2864-2879(2013).
RN   [8]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   BIOTECHNOLOGY.
RC   STRAIN=LT2;
RX   PubMed=27063436; DOI=10.1038/srep24359;
RA   Held M., Kolb A., Perdue S., Hsu S.Y., Bloch S.E., Quin M.B.,
RA   Schmidt-Dannert C.;
RT   "Engineering formation of multiple recombinant Eut protein nanocompartments
RT   in E. coli.";
RL   Sci. Rep. 6:24359-24359(2016).
RN   [9]
RP   FUNCTION.
RC   STRAIN=SL1344;
RX   PubMed=29531136; DOI=10.1128/iai.00172-18;
RA   Anderson C.J., Satkovich J., Koeseoglu V.K., Agaisse H., Kendall M.M.;
RT   "The Ethanolamine Permease EutH Promotes Vacuole Adaptation of Salmonella
RT   enterica and Listeria monocytogenes during Macrophage Infection.";
RL   Infect. Immun. 86:0-0(2018).
CC   -!- FUNCTION: A component of the bacterial microcompartment (BMC) shell
CC       dedicated to ethanolamine degradation (PubMed:22428024,
CC       PubMed:27063436). Forms a hexagonal trimer with 3 small channels and a
CC       large central pore that has been seen in both open and closed forms and
CC       is probably used for gated transport into and out of the BMC (By
CC       similarity). Ethanolamine-binding by the small channels 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 (By similarity). Expression of eutK,
CC       eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a
CC       single BMC (PubMed:22428024, PubMed:27063436). Coexpression of eutQ
CC       with eutSMNLK permits E.coli to make cells with more than one mobile
CC       BMC, as is usual in vivo (PubMed:27063436).
CC       {ECO:0000250|UniProtKB:P76541, ECO:0000250|UniProtKB:Q8XLZ0,
CC       ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436}.
CC   -!- FUNCTION: The ethanolamine (EA) catabolic bacterial microcompartment
CC       (BMC) probably concentrates low levels of ethanolamine catabolic
CC       enzymes, concentrates volatile reaction intermediates, keeps the level
CC       of toxic acetaldehyde low, generates enough acetyl-CoA to support cell
CC       growth, and maintains a pool of free coenzyme A (CoA) and NAD
CC       (Probable) (PubMed:16585748). Deletion of BMC genes (eutK, eutL, eutM)
CC       restores growth of eutD deletions, suggesting there are dedicated pools
CC       of coenzyme A (CoA) and NAD in the BMC (PubMed:23585538).
CC       {ECO:0000269|PubMed:16585748, ECO:0000269|PubMed:23585538,
CC       ECO:0000305|PubMed:10464203, ECO:0000305|PubMed:16291677,
CC       ECO:0000305|PubMed:23585538}.
CC   -!- FUNCTION: Expression of the eut operon allows this bacteria to use
CC       ethanolamine as a carbon, nitrogen and energy source. It relies on
CC       cobalamin (vitamin B12) both as a cofactor for the ethanolamine
CC       ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078).
CC       EA enhances bacterial survival in macrophages in a concentration-
CC       dependent manner, suggesting it is an important nutrient during
CC       infection (PubMed:29531136). {ECO:0000269|PubMed:29531136,
CC       ECO:0000269|PubMed:3045078}.
CC   -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC       {ECO:0000269|PubMed:3045078}.
CC   -!- SUBUNIT: Homotrimerizes to form a pseudohexamer.
CC       {ECO:0000250|UniProtKB:P76541}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000269|PubMed:27063436}.
CC   -!- INDUCTION: Part of the 17-gene eut operon transcribed from a single
CC       promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl,
CC       vitamin B12). {ECO:0000269|PubMed:3045078}.
CC   -!- DOMAIN: Has 2 BMC domains which can evolve independently of each other.
CC       {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Not required for aerobic growth on ethanolamine
CC       (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203). A
CC       double eutL-eutK strain grows as well as wild-type on EA and
CC       cyanocobalamin, but a quadruple eutL-eutK eutM-eutN strain does not
CC       grow (PubMed:16291677). A non-polar deletion mutant grows on EA at pH
CC       5.5 to pH 7.0 but not at pH 8.0 or pH 8.5, releases increased amounts
CC       of acetaldehyde on EA plus vitamin B12. Preventing acetaldehyde vapor
CC       loss allow growth up to pH 8.5 (PubMed:16585748).
CC       {ECO:0000269|PubMed:10464203, ECO:0000269|PubMed:16291677,
CC       ECO:0000269|PubMed:16585748}.
CC   -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC       eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins
CC       can be targeted to them and beta-galactosidase (lacZ) was active within
CC       the BMC, showing the BMC allows passage of substrate into the interior.
CC       This can lead to the development of tailored BMCs for specific
CC       metabolic reactions (PubMed:22428024). The addition of eutQ to the
CC       eutSMNLK construct results in biogenesis of multiple BMCs
CC       (PubMed:27063436). {ECO:0000269|PubMed:22428024,
CC       ECO:0000269|PubMed:27063436}.
CC   -!- MISCELLANEOUS: The need for a bacterial microcompartment in EA
CC       metabolism can be bypassed by increasing the levels of EAL and an
CC       acetaldehyde dehydrogenase (not necessarily EutE).
CC       {ECO:0000269|PubMed:16291677}.
CC   -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01279}.
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DR   EMBL; AF093749; AAC78125.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21350.1; -; Genomic_DNA.
DR   RefSeq; NP_461391.1; NC_003197.2.
DR   RefSeq; WP_001111056.1; NC_003197.2.
DR   AlphaFoldDB; P0A1C9; -.
DR   SMR; P0A1C9; -.
DR   STRING; 99287.STM2456; -.
DR   PaxDb; 99287-STM2456; -.
DR   GeneID; 1253978; -.
DR   KEGG; stm:STM2456; -.
DR   PATRIC; fig|99287.12.peg.2594; -.
DR   HOGENOM; CLU_1270774_0_0_6; -.
DR   OMA; HCISRTG; -.
DR   PhylomeDB; P0A1C9; -.
DR   BioCyc; SENT99287:STM2456-MONOMER; -.
DR   UniPathway; UPA00560; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IDA:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB.
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   Bacterial microcompartment; Reference proteome; Virulence.
FT   CHAIN           1..219
FT                   /note="Bacterial microcompartment shell protein EutL"
FT                   /id="PRO_0000201518"
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
//