EUTL_SALTY
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 03-AUG-2022, entry version 79.
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; Proteobacteria; 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; P0A1C9; -.
DR EnsemblBacteria; AAL21350; AAL21350; STM2456.
DR GeneID; 1253978; -.
DR KEGG; stm:STM2456; -.
DR PATRIC; fig|99287.12.peg.2594; -.
DR HOGENOM; CLU_1270774_0_0_6; -.
DR OMA; ACFYSAN; -.
DR PhylomeDB; P0A1C9; -.
DR BioCyc; SENT99287:STM2456-MON; -.
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 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 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
