EUTR_SALTY
ID EUTR_SALTY Reviewed; 350 AA.
AC Q9ZFU7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=HTH-type DNA-binding transcriptional activator EutR {ECO:0000305};
DE AltName: Full=Ethanolamine operon regulatory protein;
GN Name=eutR {ECO:0000303|PubMed:2656649}; OrderedLocusNames=STM2454;
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 INDUCTION.
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=2656649; DOI=10.1128/jb.171.6.3316-3323.1989;
RA Roof D.M., Roth J.R.;
RT "Functions required for vitamin B12-dependent ethanolamine utilization in
RT Salmonella typhimurium.";
RL J. Bacteriol. 171:3316-3323(1989).
RN [5]
RP FUNCTION, PATHWAY, AND INDUCTION BY ETHANOLAMINE AND COBALAMIN.
RC STRAIN=LT2;
RX PubMed=1328159; DOI=10.1128/jb.174.20.6634-6643.1992;
RA Roof D.M., Roth J.R.;
RT "Autogenous regulation of ethanolamine utilization by a transcriptional
RT activator of the eut operon in Salmonella typhimurium.";
RL J. Bacteriol. 174:6634-6643(1992).
RN [6]
RP FUNCTION, AND INDUCTION BY ETHANOLAMINE AND ADENOSYLCOBALAMIN.
RC STRAIN=LT2;
RX PubMed=8113167; DOI=10.1128/jb.176.5.1287-1296.1994;
RA Sheppard D.E., Roth J.R.;
RT "A rationale for autoinduction of a transcriptional activator: ethanolamine
RT ammonia-lyase (EutBC) and the operon activator (EutR) compete for adenosyl-
RT cobalamin in Salmonella typhimurium.";
RL J. Bacteriol. 176:1287-1296(1994).
RN [7]
RP FUNCTION, REGULON, INDUCTION IN MACROPHAGES AND DURING MOUSE INFECTION,
RP DISRUPTION PHENOTYPE, AND DNA-BINDING.
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 [8]
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 [9]
RP DISRUPTION PHENOTYPE.
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: Activates the transcription of the eut operon, allowing
CC utilization of ethanolamine (EA). Positively regulates its own
CC transcription (Probable) (PubMed:1328159, PubMed:8113167). Probably
CC binds EA and vitamin B12 as effectors (Probable). Competes with
CC ethanolamine ammonia-lysase (EAL, the first enzyme in the EA
CC degradation pathway) for adenosylcobalamin (PubMed:8113167).
CC Ethanolamine-associated signaling mediated via this protein, but not EA
CC degradation, impacts S.typhimurium survival within macrophages. Binds
CC the promoter of ssrB and eutS in vitro; in mouse infection models
CC binding to ssrB probably induces all 4 operons of pathogenicity island
CC SPI-2 (PubMed:26565973). {ECO:0000269|PubMed:1328159,
CC ECO:0000269|PubMed:26565973, ECO:0000269|PubMed:8113167,
CC ECO:0000305|PubMed:1328159, ECO:0000305|PubMed:2656649,
CC ECO:0000305|PubMed:8113167}.
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 in infection
CC (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, positively regulates its own expression, induced by
CC ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12). This is the
CC last gene in the operon and has a second weaker promoter that is
CC constitutively transcribed at a low level (PubMed:10464203,
CC PubMed:3045078, PubMed:1328159, PubMed:26565973) (Probable). Subject to
CC catabolite repression; expression is substantially lower during growth
CC on glucose than during growth versus succinate. Catabolite repression
CC is overcome by adding exogenous cAMP to the glucose growth media
CC (PubMed:1328159). Induced after phagocytosis by mouse RAW macrophages
CC and in spleen in mouse infection; the whole eut operon is not induced
CC (PubMed:26565973). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:1328159, ECO:0000269|PubMed:26565973,
CC ECO:0000269|PubMed:3045078, ECO:0000305|PubMed:2656649}.
CC -!- DISRUPTION PHENOTYPE: Mutations prevent expression of the entire eut
CC operon (PubMed:2656649). No phenotype during bacterial growth in vitro.
CC About 10-fold outcompeted by wild-type in mouse intestines at 2 and 4
CC days following oral infection. Loss of induction of pathogenicity
CC island SPI-2 in mouse macrophages (PubMed:26684793). About 25%
CC reduction in survival in mouse macrophage assays. Bacteria growth is
CC not enhanced by exogenous EA in macrophage survival assays
CC (PubMed:29531136). {ECO:0000269|PubMed:2656649,
CC ECO:0000269|PubMed:26684793, ECO:0000269|PubMed:29531136}.
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DR EMBL; AF093749; AAC78127.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21348.1; -; Genomic_DNA.
DR RefSeq; NP_461389.1; NC_003197.2.
DR RefSeq; WP_000753665.1; NC_003197.2.
DR AlphaFoldDB; Q9ZFU7; -.
DR SMR; Q9ZFU7; -.
DR STRING; 99287.STM2454; -.
DR PaxDb; Q9ZFU7; -.
DR EnsemblBacteria; AAL21348; AAL21348; STM2454.
DR GeneID; 1253976; -.
DR KEGG; stm:STM2454; -.
DR PATRIC; fig|99287.12.peg.2592; -.
DR HOGENOM; CLU_047930_2_0_6; -.
DR OMA; FLHHPER; -.
DR PhylomeDB; Q9ZFU7; -.
DR BioCyc; SENT99287:STM2454-MON; -.
DR UniPathway; UPA00560; -.
DR PHI-base; PHI:5299; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR Pfam; PF12833; HTH_18; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..350
FT /note="HTH-type DNA-binding transcriptional activator EutR"
FT /id="PRO_0000194510"
FT DOMAIN 243..344
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 260..281
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 311..334
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
SQ SEQUENCE 350 AA; 40055 MW; 74963E76E2DAF186 CRC64;
MKKTRTANLH HLYHEALPED VKLTPRVEVD NVHQRRTTDV YEHALTITAW QQIYDQLHPG
KFHGEFTEIL LDEIQVFREY TGLALRQSCL VWPNSFWFGI PATRGEQGFI GAQGLGSAEI
ATRPGGTEFE LSTPDDYTIL GVVISEDVIS RQATFLHNPE RVLHMLRNQL ALEVKEQHKA
ALWGFVQQAL ATFSESPETL HQPAVRKVLS DNLLLAMGTM LEEAKPIHSA ESISHQGYRR
LLSRAREYVL ENMSEPLTVL DLCNQLHVSR RTLQNAFHAI LGIGPNAWLK RIRLNAVRRE
LISPWSQSAT VKDAAMQWGF WHLGQFATDY QQLFAEKPSL TLHQRMRQWA
