EUTJ_SALTY
ID EUTJ_SALTY Reviewed; 279 AA.
AC P0A206; P41794;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ethanolamine utilization protein EutJ;
GN Name=eutJ {ECO:0000303|PubMed:7868611}; OrderedLocusNames=STM2462;
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 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], FUNCTION, 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 [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 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.
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 [7]
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: May protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from
CC inhibition, may functin in assembling the bacterial microcompartment
CC and/or in refolding EAL, suggesting it may have chaperone activity
CC (Probable). Overexpression of eutJ and eutS in E.coli leads to multiple
CC BMC-like structures; eutS expression alone leads to 1 BMC-like
CC structure per cell (PubMed:27063436). {ECO:0000269|PubMed:27063436,
CC ECO:0000305|PubMed:10464203, 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 -!- 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). A double eutJ-eutG
CC deletion is not required for growth in the above conditions. A double
CC eutG-eutH deletion is not required for growth in the above conditions.
CC Slightly attenuated in a mouse model of infection (PubMed:10464203). A
CC non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does
CC not grow at pH 8.5, no change in acetaldehyde release on EA plus
CC vitamin B12 (PubMed:16585748). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:16585748}.
CC -!- SIMILARITY: Belongs to the EutJ family. {ECO:0000305}.
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DR EMBL; U18560; AAA80210.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78119.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21356.1; -; Genomic_DNA.
DR RefSeq; NP_461397.1; NC_003197.2.
DR RefSeq; WP_000929675.1; NC_003197.2.
DR AlphaFoldDB; P0A206; -.
DR SMR; P0A206; -.
DR STRING; 99287.STM2462; -.
DR PaxDb; P0A206; -.
DR PRIDE; P0A206; -.
DR DNASU; 1253984; -.
DR EnsemblBacteria; AAL21356; AAL21356; STM2462.
DR GeneID; 1253984; -.
DR KEGG; stm:STM2462; -.
DR PATRIC; fig|99287.12.peg.2600; -.
DR HOGENOM; CLU_088869_0_0_6; -.
DR OMA; HAGEIWP; -.
DR PhylomeDB; P0A206; -.
DR BioCyc; SENT99287:STM2462-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013366; EutJ.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02529; EutJ; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Reference proteome.
FT CHAIN 1..279
FT /note="Ethanolamine utilization protein EutJ"
FT /id="PRO_0000087090"
SQ SEQUENCE 279 AA; 30018 MW; 28B8CD89141D8D90 CRC64;
MAHDEQLWLT PRLQKAAALC NQTPAASDTP LWLGVDLGTC DVVSMVVDGN AQPVAVCLDW
ADVVRDGIVW DFFGAVTLVR RHLDTLEQQL GCRFTHAATS FPPGTDPRIS INVLESAGLE
VSHVLDEPTA VADLLALDNA GVVDIGGGTT GIAIVKQGKV TYSADEATGG HHISLTLAGN
RRIPLEEAEQ YKRSNAQEIW PVVKPVYEKM AEIVARHIEG QGIADLWLAG GSCMQPGVEA
LFRQRFPELQ VHLPQHSLFM TPLAIANSGR AKAEGLYAS