EUTH_SALTY
ID EUTH_SALTY Reviewed; 408 AA.
AC P41796; P45692; Q9ZFV3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable ethanolamine permease EutH {ECO:0000305};
DE AltName: Full=Ethanolamine utilization protein EutH;
GN Name=eutH {ECO:0000303|PubMed:7868611}; OrderedLocusNames=STM2460;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
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 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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=15466042; DOI=10.1128/jb.186.20.6885-6890.2004;
RA Penrod J.T., Mace C.C., Roth J.R.;
RT "A pH-sensitive function and phenotype: evidence that EutH facilitates
RT diffusion of uncharged ethanolamine in Salmonella enterica.";
RL J. Bacteriol. 186:6885-6890(2004).
RN [6]
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 [7]
RP FUNCTION, AND 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: Probably involved in the diffusion of protonated ethanolamine
CC (EA) into the cell at low pH. At low pH most EA is protonated, and this
CC permease becomes necessary (Probable). Contributes to bacterial
CC survival and replication in acidified macrophage vacuoles, but not to
CC bacterial uptake by macrophages (PubMed:29531136).
CC {ECO:0000269|PubMed:29531136, ECO:0000305|PubMed:15466042,
CC 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:15466042}; Multi-pass membrane protein
CC {ECO:0000250}.
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: Unable to grow with ethanolamine (EA) as sole
CC carbon source. Slightly attenuated in a mouse model of infection
CC (PubMed:7868611). A double eutG-eutH deletion is not impaired for
CC aerobic growth on EA supplemented with cobalamin (vitamin B12)
CC (PubMed:10464203). Cells are unable to grow on EA at low pH
CC (PubMed:15466042). A non-polar deletion mutant does not grow on EA at
CC pH 5.5 or pH 8.5, poorly at pH 6.0 but wild-type at pH 7.0 and pH 8.0,
CC slight decrease in acetaldehyde release on EA plus vitamin B12
CC (PubMed:16585748). About 25% reduction in survival in mouse macrophage
CC assays. Bacterial growth is not enhanced by exogenous EA in macrophage
CC survival assays. Decreased survival in mouse intraperitoneal infection,
CC no phenotype in mouse colitis infections (PubMed:29531136).
CC {ECO:0000269|PubMed:10464203, ECO:0000269|PubMed:15466042,
CC ECO:0000269|PubMed:16585748, ECO:0000269|PubMed:29531136,
CC ECO:0000269|PubMed:7868611}.
CC -!- SIMILARITY: Belongs to the EutH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80212.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18560; AAA80212.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF093749; AAC78121.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21354.1; -; Genomic_DNA.
DR RefSeq; NP_461395.1; NC_003197.2.
DR RefSeq; WP_000512359.1; NC_003197.2.
DR AlphaFoldDB; P41796; -.
DR STRING; 99287.STM2460; -.
DR TCDB; 9.A.28.1.1; the ethanolamine facilitator (eaf) family.
DR PaxDb; P41796; -.
DR PRIDE; P41796; -.
DR EnsemblBacteria; AAL21354; AAL21354; STM2460.
DR GeneID; 1253982; -.
DR KEGG; stm:STM2460; -.
DR PATRIC; fig|99287.12.peg.2598; -.
DR HOGENOM; CLU_061142_0_0_6; -.
DR OMA; FGDHLGF; -.
DR PhylomeDB; P41796; -.
DR BioCyc; SENT99287:STM2460-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0034228; F:ethanolamine transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR007441; EutH.
DR PANTHER; PTHR40089; PTHR40089; 1.
DR Pfam; PF04346; EutH; 1.
DR PIRSF; PIRSF019466; EutH; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Virulence.
FT CHAIN 1..408
FT /note="Probable ethanolamine permease EutH"
FT /id="PRO_0000087087"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 68..72
FT /note="LAPVL -> GAGV (in Ref. 1; AAA80212 and 2; AAC78121)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="A -> AGRPFRLRA (in Ref. 1; AAA80212 and 2;
FT AAC78121)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="A -> G (in Ref. 2; AAC78121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 42827 MW; E27AA6E659852AF2 CRC64;
MGINEIIMYI MMFFMLIAAV DRILSQFGGS ARFLGKFGKS IEGSGGQFEE GFMAMGALGL
AMVGMTALAP VLAHVLGPVI IPVYEMLGAN PSMFAGTLLA CDMGGFFLAK ELAGGDVAAW
LYSGLILGSM MGPTIVFSIP VALGIIEPSD RRYLALGVLA GIVTIPIGCI AGGLIAMYSG
VQINGQPVEF TFALILMNMI PVLIVAVLVA LGLKFIPEKM INGFQIFAKF LVALITIGLA
AAVVKFLLGW ELIPGLDPIF MAPGDKPGEV MRAIEVIGSI SCVLLGAYPM VLLLTRWFEK
PLMNVGKLLN VNNIAAAGMV ATLANNIPMF GMMKQMDTRG KVINCAFAVS AAFALGDHLG
FAAANMNAMI FPMIVGKLIG GVTAIGVAMM LVPKDDAAQV KTEAEAQS
