EUTS_SALTY
ID EUTS_SALTY Reviewed; 111 AA.
AC Q9ZFV7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Bacterial microcompartment shell protein EutS;
DE AltName: Full=Ethanolamine utilization protein EutS;
GN Name=eutS; OrderedLocusNames=STM2470;
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 EXPRESSION IN MOUSE INFECTION.
RC STRAIN=SL1344;
RX PubMed=26565973; DOI=10.1371/journal.ppat.1005278;
RA Anderson C.J., Clark D.E., Adli M., Kendall M.M.;
RT "Ethanolamine Signaling Promotes Salmonella Niche Recognition and
RT Adaptation during Infection.";
RL PLoS Pathog. 11:e1005278-e1005278(2015).
RN [7]
RP ERRATUM OF PUBMED:26565973.
RX PubMed=26684793; DOI=10.1371/journal.ppat.1005365;
RA Anderson C.J., Clark D.E., Adli M., Kendall M.M.;
RT "Correction: Ethanolamine Signaling Promotes Salmonella Niche Recognition
RT and Adaptation during Infection.";
RL PLoS Pathog. 11:e1005365-e1005365(2015).
RN [8]
RP FUNCTION, INTERACTION WITH EUTC, SUBUNIT, SUBCELLULAR LOCATION,
RP BIOTECHNOLOGY, AND MUTAGENESIS OF GLY-39.
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 [9]
RP FUNCTION.
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 [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR
RP LOCATION, AND 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 [11]
RP FUNCTION, INTERACTION WITH EUTE, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF LEU-29 AND LYS-32.
RC STRAIN=LT2;
RX PubMed=27450681; DOI=10.1007/s00253-016-7737-8;
RA Quin M.B., Perdue S.A., Hsu S.Y., Schmidt-Dannert C.;
RT "Encapsulation of multiple cargo proteins within recombinant Eut
RT nanocompartments.";
RL Appl. Microbiol. Biotechnol. 100:9187-9200(2016).
RN [12]
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 probably major component of the bacterial microcompartment
CC (BMC) shell dedicated to ethanolamine degradation. Expression of eutK,
CC eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a
CC single BMC; expression of this protein alone can also form BMCs (which
CC may be less tightly closed than eutSMNLK shells). The 'bent' shape of
CC this subunit is required for integration of cargo proteins into these
CC BMCs (PubMed:22428024). Coexpression of eutQ with eutSMNLK permits
CC E.coli to make cells with more than one mobile BMC, as is usual in vivo
CC (PubMed:27063436). Targets at least 2 proteins (EutC and EutE) to the
CC interior of the BMC (PubMed:22428024, PubMed:27063436,
CC PubMed:27450681). Proteins such as EutS containing circularly permuted
CC BMC domains may play a key role in conferring heterogeneity and
CC flexibility in this BMC (Probable). {ECO:0000269|PubMed:22428024,
CC ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:27450681, ECO:0000305}.
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 {ECO:0000269|PubMed:16585748, ECO:0000305|PubMed:10464203,
CC ECO:0000305|PubMed:16291677, 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: Homohexamer with a central pore; the hexamer is probably bent
CC by about 40 degrees rather that symmetric; bending depends on Gly-39
CC (Probable). Interacts with the N-terminus of EutC, targeting it to the
CC interior of the BMC (PubMed:22428024, PubMed:27063436,
CC PubMed:27450681). Interacts with the N-terminus of EutE, targeting it
CC to the interior of the BMC (PubMed:27450681).
CC {ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436,
CC ECO:0000269|PubMed:27450681, ECO:0000305|PubMed:22428024}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436,
CC ECO:0000269|PubMed:27450681}.
CC -!- INDUCTION: The first gene of the 17-gene eut operon transcribed from a
CC single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl,
CC vitamin B12) (PubMed:3045078). Expressed at low levels following mouse
CC infection, not induced in infected macrophages or in spleen
CC (PubMed:26565973). {ECO:0000269|PubMed:26565973,
CC ECO:0000269|PubMed:3045078}.
CC -!- DOMAIN: Adding an N- or C-terminal His-tag to this protein prevents it
CC forming BMCs (PubMed:27450681). One side of the hexamer is concave and
CC lined by hydrophobic residues, the other side has a slightly
CC protruding, 6-stranded beta-barrel (By similarity).
CC {ECO:0000250|UniProtKB:P63746, ECO:0000269|PubMed:27450681}.
CC -!- DISRUPTION PHENOTYPE: Not required for aerobic growth on ethanolamine
CC (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203,
CC PubMed:16291677). A non-polar deletion mutant grows on EA from pH 5.5
CC to pH 8.0, but does not grow at pH 8.5, releases increased amounts of
CC acetaldehyde on EA plus vitamin B12 (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 both BMCs; beta-galactosidase (lacZ) was active
CC within the BMC, showing the BMC allows passage of substrate into the
CC interior. This can lead to the development of tailored BMCs for
CC specific metabolic reactions (PubMed:22428024, PubMed:27063436). The
CC addition of eutQ to the eutSMNLK construct results in biogenesis of
CC multiple BMCs (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 EutS/PduU family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF093749; AAC78111.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21364.1; -; Genomic_DNA.
DR RefSeq; NP_461405.1; NC_003197.2.
DR RefSeq; WP_001031445.1; NC_003197.2.
DR AlphaFoldDB; Q9ZFV7; -.
DR SMR; Q9ZFV7; -.
DR STRING; 99287.STM2470; -.
DR PaxDb; Q9ZFV7; -.
DR EnsemblBacteria; AAL21364; AAL21364; STM2470.
DR GeneID; 1253992; -.
DR KEGG; stm:STM2470; -.
DR PATRIC; fig|99287.12.peg.2608; -.
DR HOGENOM; CLU_143326_0_0_6; -.
DR OMA; AMIAIND; -.
DR PhylomeDB; Q9ZFV7; -.
DR BioCyc; SENT99287:STM2470-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IDA:UniProtKB.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07046; BMC_PduU-EutS; 1.
DR Gene3D; 3.30.70.1710; -; 1.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR009307; EutS/PduU/CutR.
DR PANTHER; PTHR40449; PTHR40449; 1.
DR Pfam; PF00936; BMC; 1.
DR PIRSF; PIRSF012296; EutS_PduU; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS51931; BMC_CP; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Reference proteome; Virulence.
FT CHAIN 1..111
FT /note="Bacterial microcompartment shell protein EutS"
FT /id="PRO_0000201523"
FT DOMAIN 5..103
FT /note="BMC circularly permuted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT MUTAGEN 29
FT /note="L->A: EutC and EutE constructs are no longer
FT targeted to EutS or eutSMNLK BMCs. BMCs are formed in
FT E.coli by both sets of genes."
FT /evidence="ECO:0000269|PubMed:27450681"
FT MUTAGEN 32
FT /note="K->A: EutC constructs are targeted to EutS BMCs,
FT cells are somewhat elongated."
FT /evidence="ECO:0000269|PubMed:27450681"
FT MUTAGEN 39
FT /note="G->V: No longer targets EutC-tagged constructs to
FT BMCs, probably forms flat symmetric hexamers."
FT /evidence="ECO:0000269|PubMed:22428024"
SQ SEQUENCE 111 AA; 11673 MW; D86D4E96A576CA4E CRC64;
MNKERIIQEF VPGKQVTLAH LIAHPGEELA KKIGVPDAGA IGIMTLTPGE TAMIAGDLAM
KAADVHIGFL DRFSGALVIY GTVGAVEEAL LQTVSGLGRL LNFTLCELTK S
