EUTQ_SALTY
ID EUTQ_SALTY Reviewed; 229 AA.
AC Q9ZFV5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Acetate kinase EutQ {ECO:0000303|PubMed:26448059};
DE EC=2.7.2.1 {ECO:0000269|PubMed:26448059};
DE AltName: Full=Ethanolamine utilization protein EutQ;
GN Name=eutQ; OrderedLocusNames=STM2468;
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 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 [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 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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, NO COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, PROBABLE SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-172; 173-GLU--ASP-175; GLU-173 AND
RP ASP-175.
RC STRAIN=LT2;
RX PubMed=26448059; DOI=10.1111/mmi.13243;
RA Moore T.C., Escalante-Semerena J.C.;
RT "The EutQ and EutP proteins are novel acetate kinases involved in
RT ethanolamine catabolism: physiological implications for the function of the
RT ethanolamine metabolosome in Salmonella enterica.";
RL Mol. Microbiol. 99:497-511(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).
RN [8]
RP FUNCTION, INTERACTION WITH EUTM, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, 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 [9] {ECO:0007744|PDB:2PYT}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 98-229, AND SUBUNIT.
RG Joint Center For Structural Genomics (JCSG);
RT "Crystal structure of Ethanolamine utilization protein eutQ (16421009) from
RT Salmonella typhimurium LT2 at 1.90 A resolution.";
RL Submitted (MAY-2007) to the PDB data bank.
CC -!- FUNCTION: A bidirectional acetate kinase that may drive flux through
CC the ethanolamine (EA) degradation pathway under anoxic conditions found
CC when this bacteria infects the host intestine. It may generate ATP that
CC can be used by other enzymes (EutA and EutT) in the eut pathway. Can
CC use GTP instead of ATP with reduced efficiency (PubMed:26448059). Might
CC be required to correctly target EutE to bacterial microcompartments
CC (BMC) (Probable). Required for the biogenesis of multiple mobile BMCs
CC per cell. Might serve as an assembly hub for BMC shell proteins.
CC Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads
CC to formation of a single BMC; coexpression of eutQ with eutSMNLK
CC permits E.coli to make cells with more than one mobile BMC, as is usual
CC in vivo. EutS alone also forms BMCs, but in the presence of eutQ both
CC BMCs and protein filaments are formed (PubMed:27063436).
CC {ECO:0000269|PubMed:26448059, ECO:0000269|PubMed:27063436,
CC ECO:0000305|PubMed:23585538}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.2.1;
CC Evidence={ECO:0000269|PubMed:26448059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11353;
CC Evidence={ECO:0000269|PubMed:26448059};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11354;
CC Evidence={ECO:0000269|PubMed:26448059};
CC -!- COFACTOR:
CC Note=Does not need divalent cations. {ECO:0000269|PubMed:26448059};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for acetate {ECO:0000269|PubMed:26448059};
CC KM=0.5 mM for ATP {ECO:0000269|PubMed:26448059};
CC Note=kcat is 318 sec(-1). {ECO:0000269|PubMed:26448059};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000269|PubMed:3045078}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with the N-terminus of EutM; a
CC probably cytoplasm-facing helix (EutM 'Val-49' to 'Gln-64') interacts
CC with N-terminus of EutQ (PubMed:27063436).
CC {ECO:0000269|PubMed:27063436, ECO:0000305|Ref.9}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:26448059, ECO:0000305|PubMed:27063436}. Note=May be
CC found on the cytoplasmic face of the BMC.
CC {ECO:0000305|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: A quadruple eutP-eutQ-eutT-eutD deletion is not
CC impaired for aerobic growth on ethanolamine (EA) supplemented with
CC cobalamin (vitamin B12) (PubMed:10464203). A non-polar deletion mutant
CC grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5,
CC releases increased amounts of acetaldehyde on EA plus vitamin B12
CC (PubMed:16585748). Does not grow on EA and tetrathionate under anoxic
CC conditions; complemented by acetate/propionate kinases AckA, PduW or
CC TdcD (PubMed:26448059). Only makes a single immobile BMC localized near
CC the cell pole (PubMed:27063436). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:16585748, ECO:0000269|PubMed:26448059,
CC ECO:0000269|PubMed:27063436}.
CC -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC eutK, eutL, eutM, eutN, eutS (eutSMNLK). Cargo proteins can be targeted
CC to them. The addition of eutQ to the eutSMNLK construct results in
CC biogenesis of multiple BMCs. This can lead to the development of
CC tailored BMCs for specific metabolic reactions.
CC {ECO:0000269|PubMed:27063436}.
CC -!- SIMILARITY: Belongs to the EutQ cupin-like family. {ECO:0000305}.
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DR EMBL; AF093749; AAC78113.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21362.1; -; Genomic_DNA.
DR RefSeq; NP_461403.1; NC_003197.2.
DR RefSeq; WP_000733867.1; NC_003197.2.
DR PDB; 2PYT; X-ray; 1.90 A; A/B=98-229.
DR PDBsum; 2PYT; -.
DR AlphaFoldDB; Q9ZFV5; -.
DR SMR; Q9ZFV5; -.
DR STRING; 99287.STM2468; -.
DR PaxDb; Q9ZFV5; -.
DR DNASU; 1253990; -.
DR EnsemblBacteria; AAL21362; AAL21362; STM2468.
DR GeneID; 1253990; -.
DR KEGG; stm:STM2468; -.
DR PATRIC; fig|99287.12.peg.2606; -.
DR HOGENOM; CLU_082122_0_0_6; -.
DR OMA; SKVTWSS; -.
DR PhylomeDB; Q9ZFV5; -.
DR BioCyc; MetaCyc:STM2468-MON; -.
DR BioCyc; SENT99287:STM2468-MON; -.
DR UniPathway; UPA00560; -.
DR EvolutionaryTrace; Q9ZFV5; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IPI:UniProtKB.
DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR010424; EutQ.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR36169; PTHR36169; 1.
DR Pfam; PF06249; EutQ; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Bacterial microcompartment; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase; Virulence.
FT CHAIN 1..229
FT /note="Acetate kinase EutQ"
FT /id="PRO_0000087098"
FT REGION 1..100
FT /note="Required for interaction with EutM"
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 172
FT /note="D->A: Complements deletion as well as wild-type."
FT /evidence="ECO:0000269|PubMed:26448059"
FT MUTAGEN 173..175
FT /note="EID->AIA: Slight reduction in complementation of
FT deletion."
FT /evidence="ECO:0000269|PubMed:26448059"
FT MUTAGEN 173
FT /note="E->A: Slight reduction in complementation of
FT deletion."
FT /evidence="ECO:0000269|PubMed:26448059"
FT MUTAGEN 175
FT /note="D->A: Complements deletion as well as wild-type."
FT /evidence="ECO:0000269|PubMed:26448059"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2PYT"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2PYT"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2PYT"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2PYT"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2PYT"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2PYT"
FT STRAND 152..168
FT /evidence="ECO:0007829|PDB:2PYT"
FT STRAND 170..186
FT /evidence="ECO:0007829|PDB:2PYT"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2PYT"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2PYT"
FT STRAND 206..223
FT /evidence="ECO:0007829|PDB:2PYT"
SQ SEQUENCE 229 AA; 24992 MW; 75ADAC10E5F88279 CRC64;
MKKLITANDI RAAHARGEQA MSVVLRASII TPEAREVAEL LGFTITECDE SVPASTSAQA
CKSESQRIRE AIIAQLPEGQ FTESLVAQLM EKVLKEKQSL ELGTMQPSFT SVTGKGGVKV
IDGSSVKFGR FDGAEPHCVG LTDLVTEQDG SSMAAGFMQW DNAFFPWTLN YDEIDMVLEG
ELHVRHEGET MIAKAGDVMF IPKGSSIEFG TPTSVRFLYV AWPANWQSV
