EUTK_SALTY
ID EUTK_SALTY Reviewed; 164 AA.
AC Q9ZFU8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bacterial microcompartment shell protein EutK;
DE AltName: Full=Ethanolamine utilization protein EutK;
GN Name=eutK; OrderedLocusNames=STM2455;
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], POSSIBLE FUNCTION, AND DISRUPTION
RP 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. Expression of eutK, eutL, eutM,
CC eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC
CC (PubMed:22428024, PubMed:27063436). Coexpression of eutQ with eutSMNLK
CC permits E.coli to make cells with more than one mobile BMC, as is usual
CC in vivo (PubMed:27063436). {ECO:0000269|PubMed:22428024,
CC 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: Monomeric in solution. {ECO:0000250|UniProtKB:P76540}.
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 -!- 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, PubMed:27063436). The addition of
CC eutQ to the 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 bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278}.
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DR EMBL; AF093749; AAC78126.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21349.1; -; Genomic_DNA.
DR RefSeq; NP_461390.1; NC_003197.2.
DR RefSeq; WP_000606266.1; NC_003197.2.
DR AlphaFoldDB; Q9ZFU8; -.
DR SMR; Q9ZFU8; -.
DR STRING; 99287.STM2455; -.
DR PaxDb; Q9ZFU8; -.
DR EnsemblBacteria; AAL21349; AAL21349; STM2455.
DR GeneID; 1253977; -.
DR KEGG; stm:STM2455; -.
DR PATRIC; fig|99287.12.peg.2593; -.
DR HOGENOM; CLU_064903_7_0_6; -.
DR OMA; WLIGGFK; -.
DR PhylomeDB; Q9ZFU8; -.
DR BioCyc; SENT99287:STM2455-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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.1710; -; 1.
DR InterPro; IPR020808; Bact_microcomp_CS.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR InterPro; IPR032298; EutK_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00936; BMC; 1.
DR Pfam; PF16365; EutK_C; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS01139; BMC_1; 1.
DR PROSITE; PS51930; BMC_2; 1.
DR PROSITE; PS51933; EUTK_C; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Reference proteome; Virulence.
FT CHAIN 1..164
FT /note="Bacterial microcompartment shell protein EutK"
FT /id="PRO_0000004785"
FT DOMAIN 4..88
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT DOMAIN 108..164
FT /note="EutK-Ctail"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01281"
FT CONFLICT 65
FT /note="Q -> K (in Ref. 1; AAC78126)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..154
FT /note="LR -> FG (in Ref. 1; AAC78126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 17486 MW; 9CA9F2DA4EACF2BC CRC64;
MINALGLLEV DGMVAAVDAA DAMLKAANVR LLSHQVLDPG RLTLVVEGDL AACRAALDAG
SAAAQRTGRV ISRKEIGRPE EDTQWLIGGF ARATTPTEKA PQVPATPEFA EALLALLASV
RQGMTAGEVA AHFGWPLEQA RNVLEQLFSD GALRKRSSRY RIKN
