MALT_VIBC1
ID MALT_VIBC1 Reviewed; 902 AA.
AC A7N5N6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
GN OrderedLocusNames=VIBHAR_04848;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000790; ABU72756.1; -; Genomic_DNA.
DR RefSeq; WP_011999152.1; NC_022270.1.
DR AlphaFoldDB; A7N5N6; -.
DR SMR; A7N5N6; -.
DR PRIDE; A7N5N6; -.
DR EnsemblBacteria; ABU72756; ABU72756; VIBHAR_04848.
DR KEGG; vha:VIBHAR_04848; -.
DR PATRIC; fig|338187.25.peg.5341; -.
DR OMA; SDWVSNA; -.
DR OrthoDB; 1377603at2; -.
DR Proteomes; UP000008152; 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; Transcription; Transcription regulation.
FT CHAIN 1..902
FT /note="HTH-type transcriptional regulator MalT"
FT /id="PRO_1000085782"
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; 103870 MW; 6FCD39F9410492FD CRC64;
MWIPSKLTRP GRLHNAIVRP RVLDLLQQAP YYKLVLFRSP AGYGKTTMAA QWLSDKPNVG
WYSIDDSDND GFRFVNYLLQ ALNKATNYNC SNAQKLAEKR QFSSLRSLFS EVFAEMADFQ
HECYVVLDDY HLITNDEIHE SMRFFLKHMP DNLTVVVTSR AAPPLGTANL RVRDLMIEIG
NEMLAFDTEE TTRFFNQRIA DGIDEDMANN LRTYVEGWPS ALQLIALQAQ HQNRTLAQTV
ESVSQFNHAH LWDYLVEEVF DLLDQETRHF LMQVSVLDHF NDELVFALTQ REDALGMIES
LNRFGLFIYP LEGEQNWFRF HNLFGEFLSH ERLARIPQQE KDLHRNAAVA WLKQKAPHQA
IHHAQKSNDT DLIVEILNEF GWKMFNQGEL TTLESAINQL DKDLLFSHPK LSMLRAWLAQ
SQHRYNQVGK LLAEAEEEHK KRNIEIDSGY QGQANALLAQ VAINSNQPEH ALELAELALS
QLDPTVYRSR IVATSVVGEV NHVLGKLDRA LPMMQQTEKL ARQYQVYHQA LWAILQQSEI
MIAQGYVQAA FELQDSGFRL IEEQQLQHVP LHEFLLRIRA QVLWCWNRLD EAEECAYKGL
QILENHSPSK HLHSYSMLAR IAIGRGELDK AGKFIEHIQH LMKQSTYHVD WTANASLSLI
LFWQARGNTE AIQEWLNTAV RPESACNHFQ QLQWRNIARA HINLGQYDEA REALDFLQSE
AHRTNLVTDT NRNLVVEAIL AARQKDEEQA KTLLKEALVM TNQTGMVGNF LTDGATIGGL
LEKLSLRHEL GDLERHRAQQ LMKDISSNQR SRSIHFDEDF IEKLVNHPNV PELVRTSPLT
QREWQVLGLI YSGFSNEQIA QELDVAGTTI KTHIRNLYQK LNIANRKEAI VTAENLLQLM
GY