MALT_VIBVY
ID MALT_VIBVY Reviewed; 902 AA.
AC Q7MG94;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=HTH-type transcriptional regulator MalT {ECO:0000255|HAMAP-Rule:MF_01247};
DE AltName: Full=ATP-dependent transcriptional activator MalT {ECO:0000255|HAMAP-Rule:MF_01247};
GN Name=malT {ECO:0000255|HAMAP-Rule:MF_01247}; OrderedLocusNames=VVA0076;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
CC -!- FUNCTION: Positively regulates the transcription of the maltose regulon
CC whose gene products are responsible for uptake and catabolism of malto-
CC oligosaccharides. Specifically binds to the promoter region of its
CC target genes, recognizing a short DNA motif called the MalT box.
CC {ECO:0000255|HAMAP-Rule:MF_01247}.
CC -!- ACTIVITY REGULATION: Activated by ATP and maltotriose, which are both
CC required for DNA binding. {ECO:0000255|HAMAP-Rule:MF_01247}.
CC -!- SUBUNIT: Monomer in solution. Oligomerizes to an active state in the
CC presence of the positive effectors ATP and maltotriose.
CC {ECO:0000255|HAMAP-Rule:MF_01247}.
CC -!- SIMILARITY: Belongs to the MalT family. {ECO:0000255|HAMAP-
CC Rule:MF_01247}.
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DR EMBL; BA000038; BAC96101.1; -; Genomic_DNA.
DR RefSeq; WP_011151506.1; NC_005140.1.
DR AlphaFoldDB; Q7MG94; -.
DR SMR; Q7MG94; -.
DR STRING; 672.VV93_v1c30870; -.
DR EnsemblBacteria; BAC96101; BAC96101; BAC96101.
DR KEGG; vvy:VVA0076; -.
DR PATRIC; fig|196600.6.peg.3297; -.
DR eggNOG; COG2909; Bacteria.
DR HOGENOM; CLU_006325_3_0_6; -.
DR OMA; SDWVSNA; -.
DR OrthoDB; 1377603at2; -.
DR Proteomes; UP000002675; Chromosome II.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045913; P:positive regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01247; HTH_type_MalT; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR041617; TPR_MalT.
DR InterPro; IPR023768; Tscrpt_reg_HTH_MalT.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF17874; TPR_MalT; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; Carbohydrate metabolism; DNA-binding;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..902
FT /note="HTH-type transcriptional regulator MalT"
FT /id="PRO_0000184172"
FT DOMAIN 832..897
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
FT DNA_BIND 856..875
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
SQ SEQUENCE 902 AA; 103847 MW; 487D977F7A84AE39 CRC64;
MWIPSKLTRP GRLHNAIVRP RVLELLQQAP YYKLVLFRSP AGYGKTTMAA QWLADKTNVG
WYSIDDSDND GFRFINYLLQ ALNKATNGNC NNAQKLAEKR QFSSLRSLFS DVFAEMVDFH
QECYVVLDDY HVINNEEVHE AMRFFLKHMP DNLTLVVTSR ANPPLGTANL RVRDLMIEIG
NEMLAFDTEE TTRFFNQRVA DGIDEDTANN LRNYVEGWPS ALQLIALQAQ HQKRTLAQSA
ESVSQFNHAH LWDYLVEEVF DLLDADTRKF LMQVSVLDHF NDELVYALTQ REDALGMIES
LNRYGLFIYP LEGEQNWFRF HNLFGEFLSH ERQARIPQQE QELNRNAAIA WLKQKSPHQA
IRHAQKAYDG ELVAEILNEF GWKMFNQGEL STLESAINLL EKDLLFSNPK LTMLRAWLAQ
SQHRYNQVGT LLAEAENEHK KRNIDLDIQY QGQANALLAQ VAINSNDPEK ALELAELALS
QLDSTVYRSR IVATSVVGEV NHVIGRLDRA LPMMQQTEKL ARQYQVYHQA LWAILQQSEI
LIAQGYVQAA FELQDSAFRL IEEQQLQHVP LHEFLLRVRA QVLWCWNRLD EAEECAYKGL
QILENHAPSK HLHSYSMLAR IAIGRGELDR AGKFIEHIQH LMKQSTYHVD WTANASLSLI
LYWQAKGKLN AIQEWLNTAV RPENACNHFC QLQWRNIARA HINLGQYDQA RQALDFLQSE
AEKANLVTDR NRNLIIEAIF AVHQKDENQA KVLLKEALQL TNQTGMVGNF LIDGATIGTL
LEKLTNRHEL GDLERHRALQ LMKDISSNQR SRSVHFDEEF VEKLVTHPNV PELVRTSPLT
QREWQVLGLI YSGFSNEQIA QELDVAGTTI KTHIRNLYQK LNIANRKEAV TTAENLLQLM
GY