EUTQ_CLOD6
ID EUTQ_CLOD6 Reviewed; 157 AA.
AC Q187N7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Acetate kinase EutQ;
DE EC=2.7.2.1 {ECO:0000250|UniProtKB:Q9ZFV5};
DE AltName: Full=Ethanolamine utilization protein EutQ {ECO:0000303|PubMed:16804543};
GN Name=eutQ; Synonyms=CD1925; OrderedLocusNames=CD630_19250;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2] {ECO:0007744|PDB:4AXO}
RP X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 17-157, FUNCTION, AND SUBUNIT.
RC STRAIN=630;
RX PubMed=23144756; DOI=10.1371/journal.pone.0048360;
RA Pitts A.C., Tuck L.R., Faulds-Pain A., Lewis R.J., Marles-Wright J.;
RT "Structural insight into the Clostridium difficile ethanolamine utilisation
RT microcompartment.";
RL PLoS ONE 7:e48360-e48360(2012).
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. Might
CC serve as an assembly hub for bacterial microcompartment (BMC) shell
CC proteins (By similarity). Overexpression in E.coli leads to lamellar
CC structures that inhibit cell division (PubMed:23144756). Expression of
CC the eut operon may allow this bacteria to use EA as a carbon, nitrogen
CC and energy source (Probable). {ECO:0000250|UniProtKB:Q9ZFV5,
CC ECO:0000269|PubMed:23144756, ECO:0000305|PubMed:23144756}.
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:0000250|UniProtKB:Q9ZFV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11353;
CC Evidence={ECO:0000250|UniProtKB:Q9ZFV5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11354;
CC Evidence={ECO:0000250|UniProtKB:Q9ZFV5};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000305|PubMed:23144756}.
CC -!- SUBUNIT: Homodimer (PubMed:23144756). May interact with EutM (By
CC similarity). {ECO:0000250|UniProtKB:Q9ZFV5,
CC ECO:0000269|PubMed:23144756}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:23144756}. Note=May be found on the cytoplasmic
CC face of the BMC. {ECO:0000250|UniProtKB:Q9ZFV5}.
CC -!- SIMILARITY: Belongs to the EutQ cupin-like family. {ECO:0000305}.
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DR EMBL; AM180355; CAJ68801.1; -; Genomic_DNA.
DR RefSeq; WP_009893336.1; NC_009089.1.
DR RefSeq; YP_001088432.1; NC_009089.1.
DR PDB; 4AXO; X-ray; 1.00 A; A/B=17-157.
DR PDBsum; 4AXO; -.
DR AlphaFoldDB; Q187N7; -.
DR SMR; Q187N7; -.
DR STRING; 272563.CD630_19250; -.
DR EnsemblBacteria; CAJ68801; CAJ68801; CD630_19250.
DR GeneID; 66354306; -.
DR KEGG; cdf:CD630_19250; -.
DR KEGG; pdc:CDIF630_02129; -.
DR PATRIC; fig|272563.120.peg.2021; -.
DR eggNOG; COG4766; Bacteria.
DR OMA; WTVLYDE; -.
DR PhylomeDB; Q187N7; -.
DR BioCyc; PDIF272563:G12WB-2069-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-EC.
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; Bacterial microcompartment; Kinase; Reference proteome;
KW Transferase.
FT CHAIN 1..157
FT /note="Acetate kinase EutQ"
FT /id="PRO_0000452917"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4AXO"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4AXO"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4AXO"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 81..95
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 97..113
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4AXO"
FT STRAND 133..149
FT /evidence="ECO:0007829|PDB:4AXO"
SQ SEQUENCE 157 AA; 17717 MW; 71EA3BC51D301166 CRC64;
MDISNIDKNL IETLVRQIIE EKISGTKDTV DFVRNKDISG ITSIKLPTVK VSESDRLDTG
NPSDVVYTKD LFTLEESPRL GCGMMEMKET TFDWTLNYDE IDYVIDGTLD IIIDGRKVSA
SSGELIFIPK GSKIQFSVPD YARFIYVTYP ADWASQN
