EUTN_SALTY
ID EUTN_SALTY Reviewed; 99 AA.
AC P41792;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Bacterial microcompartment shell vertex protein EutN {ECO:0000305};
DE AltName: Full=Ethanolamine catabolic microcompartment shell protein EutN {ECO:0000305};
DE AltName: Full=Ethanolamine utilization protein EutN;
GN Name=eutN {ECO:0000303|PubMed:10464203};
GN Synonyms=cchB {ECO:0000303|PubMed:7868611}; OrderedLocusNames=STM2464;
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 POSSIBLE FUNCTION.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=7868611; DOI=10.1128/jb.177.5.1357-1366.1995;
RA Stojiljkovic I., Baeumler A.J., Heffron F.;
RT "Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence,
RT protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG
RT eutH gene cluster.";
RL J. Bacteriol. 177:1357-1366(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POSSIBLE FUNCTION.
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, 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 [10]
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: Probably forms vertices in 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 (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). It may be involved in
CC transporting positively charged molecules into and out of the BMC (By
CC similarity). {ECO:0000250|UniProtKB:P0AEJ8,
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 {ECO:0000269|PubMed:16291677, ECO:0000269|PubMed:16585748,
CC ECO:0000305|PubMed:10464203, ECO:0000305|PubMed:16291677,
CC ECO:0000305|PubMed:23585538, ECO:0000305|PubMed:7868611}.
CC -!- FUNCTION: Expression of the eut operon allows this bacteria to use
CC ethanolamine (EA) 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: Homopentamer with a small central pore.
CC {ECO:0000250|UniProtKB:P0DUM1}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:P0AEJ8}.
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 -!- DISRUPTION PHENOTYPE: A double eutM-eutN strain grows as well as wild-
CC type on ethanolamine (EA) and cyanocobalamin, but a quadruple eutL-
CC eutK-eutM-eutN strain does not grow (PubMed:16291677). A non-polar
CC deletion mutant grows on EA at pH 5.5 to pH 7.0 but not at pH 8.0 or pH
CC 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12.
CC Preventing acetaldehyde vapor loss allow growth up to pH 8.5
CC (PubMed:16585748). {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 CcmL/EutN family. {ECO:0000305}.
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; U18560; AAA80208.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78117.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21358.1; -; Genomic_DNA.
DR RefSeq; NP_461399.3; NC_003197.2.
DR RefSeq; WP_000387009.1; NC_003197.2.
DR AlphaFoldDB; P41792; -.
DR SMR; P41792; -.
DR STRING; 99287.STM2464; -.
DR PaxDb; P41792; -.
DR EnsemblBacteria; AAL21358; AAL21358; STM2464.
DR GeneID; 1253986; -.
DR KEGG; stm:STM2464; -.
DR HOGENOM; CLU_148498_0_1_6; -.
DR PhylomeDB; P41792; -.
DR BioCyc; SENT99287:STM2464-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01614; EutN_CcmL; 1.
DR Gene3D; 2.40.50.220; -; 1.
DR InterPro; IPR004992; EutN_CcmL.
DR InterPro; IPR036677; EutN_CcmL_sf.
DR PANTHER; PTHR36539; PTHR36539; 1.
DR Pfam; PF03319; EutN_CcmL; 1.
DR SUPFAM; SSF159133; SSF159133; 1.
DR PROSITE; PS51932; BMV; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Reference proteome; Virulence.
FT CHAIN 1..99
FT /note="Bacterial microcompartment shell vertex protein
FT EutN"
FT /id="PRO_0000087093"
FT DOMAIN 5..87
FT /note="BMV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01280"
SQ SEQUENCE 99 AA; 10351 MW; 4C543D983D2A6DC7 CRC64;
MEADMKLAVV TGQIVCTVRH QGLAHDKLLM VEMIDAQGNP DGQCAVAIDS IGAGTGEWVL
LVSGSSARQA HRSELSPVDL CVIGIVDEVV AGGKVVFHK
