DHAQ_LACLA
ID DHAQ_LACLA Reviewed; 328 AA.
AC Q9CIW0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=DhaKLM operon coactivator DhaQ;
DE AltName: Full=DhaS coactivator DhaQ;
GN Name=dhaQ; OrderedLocusNames=LL0246; ORFNames=L44063;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH GLYCEROL, FUNCTION,
RP AND SUBUNIT.
RX PubMed=16760471; DOI=10.1074/jbc.m603486200;
RA Christen S., Srinivas A., Baehler P., Zeller A., Pridmore D.,
RA Bieniossek C., Baumann U., Erni B.;
RT "Regulation of the Dha operon of Lactococcus lactis: a deviation from the
RT rule followed by the Tetr family of transcription regulators.";
RL J. Biol. Chem. 281:23129-23137(2006).
CC -!- FUNCTION: Coactivator for the transcription factor DhaS. The
CC heterotetramer formed by DhaQ and DhaS functions as transcriptional
CC regulator. Activated by covalent binding of dihydroxyacetone to DhaQ.
CC The complex activates the dhaKLM operon. {ECO:0000269|PubMed:16760471}.
CC -!- SUBUNIT: Homodimer. Interacts with a homodimer of DhaS.
CC {ECO:0000269|PubMed:16760471}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK04344.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005176; AAK04344.1; ALT_INIT; Genomic_DNA.
DR PIR; F86655; F86655.
DR RefSeq; NP_266402.2; NC_002662.1.
DR RefSeq; WP_010905234.1; NC_002662.1.
DR PDB; 2IU4; X-ray; 1.96 A; A/B=1-328.
DR PDB; 2IU6; X-ray; 2.00 A; A/B=1-328.
DR PDBsum; 2IU4; -.
DR PDBsum; 2IU6; -.
DR AlphaFoldDB; Q9CIW0; -.
DR SMR; Q9CIW0; -.
DR STRING; 272623.L44063; -.
DR PaxDb; Q9CIW0; -.
DR PRIDE; Q9CIW0; -.
DR EnsemblBacteria; AAK04344; AAK04344; L44063.
DR KEGG; lla:L44063; -.
DR PATRIC; fig|272623.7.peg.271; -.
DR eggNOG; COG2376; Bacteria.
DR HOGENOM; CLU_017054_0_2_9; -.
DR OMA; DLDWVKW; -.
DR EvolutionaryTrace; Q9CIW0; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR InterPro; IPR012735; DhaK_1b.
DR InterPro; IPR004006; DhaK_dom.
DR Pfam; PF02733; Dak1; 1.
DR TIGRFAMs; TIGR02362; dhaK1b; 1.
DR PROSITE; PS51481; DHAK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..328
FT /note="DhaKLM operon coactivator DhaQ"
FT /id="PRO_0000270536"
FT DOMAIN 6..328
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT MOD_RES 215
FT /note="Tele-(1,2,3-trihydroxypropan-2-yl)histidine"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2IU4"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:2IU4"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:2IU4"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 228..243
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2IU4"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:2IU4"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:2IU4"
SQ SEQUENCE 328 AA; 36236 MW; 2DF5B1E944E953A7 CRC64;
MKFYNSTNEI PEEMLKGIDL TYPQLTYLPE TGILYDNTYN EKTVPIISGG GSGHEPAHVG
YVGSGMLAAA VTGPLFIPPK SKNILKAIRQ VNSGKGVFVI IKNFEADLKE FNEAIKEART
EGIDVRYIVS HDDISVNAYN FHKRHRGVAG TILLHKILGA FAKEGGSIDE IEQLALSLSP
EIYTLGVALA PVHFPHQKTS FVLAEDEVSF GIGIHGEPGY RVEKFEGSER IAIELVNKLK
AEINWQKKAN KNYILLVNGL GSTTLMELYS FQYDVMRLLE LEGLSVKFCK VGNLMTSCDM
SGISLTLCSV KDPKWLDYLN VPTGAFAW
