ID H5V3F1_ATLHE Unreviewed; 901 AA.
AC H5V3F1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=HTH-type transcriptional regulator MalT {ECO:0000256|HAMAP-Rule:MF_01247};
DE AltName: Full=ATP-dependent transcriptional activator MalT {ECO:0000256|HAMAP-Rule:MF_01247};
GN Name=malT {ECO:0000256|HAMAP-Rule:MF_01247,
GN ECO:0000313|EMBL:GAB52509.1};
GN ORFNames=EH105704_07_00760 {ECO:0000313|EMBL:GAB52509.1};
OS Atlantibacter hermannii NBRC 105704.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Atlantibacter.
OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB52509.1, ECO:0000313|Proteomes:UP000010297};
RN [1] {ECO:0000313|EMBL:GAB52509.1, ECO:0000313|Proteomes:UP000010297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB52509.1,
RC ECO:0000313|Proteomes:UP000010297};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL Submitted (FEB-2012) 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:0000256|HAMAP-Rule:MF_01247}.
CC -!- ACTIVITY REGULATION: Activated by ATP and maltotriose, which are both
CC required for DNA binding. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01247}.
CC -!- SIMILARITY: Belongs to the MalT family. {ECO:0000256|HAMAP-
CC Rule:MF_01247}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB52509.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAFF01000007; GAB52509.1; -; Genomic_DNA.
DR RefSeq; WP_002436479.1; NZ_BAFF01000007.1.
DR AlphaFoldDB; H5V3F1; -.
DR eggNOG; COG2909; Bacteria.
DR Proteomes; UP000010297; Unassembled WGS sequence.
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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR023768; Tscrpt_reg_HTH_MalT.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR44688; -; 1.
DR PANTHER; PTHR44688:SF7; HTH-TYPE TRANSCRIPTIONAL REGULATOR MALT; 1.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF17874; TPR_MalT; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_01247};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01247};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01247};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01247};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01247}; Reference proteome {ECO:0000313|Proteomes:UP000010297};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_01247};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01247}.
FT DOMAIN 829..894
FT /note="HTH luxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50043"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01247"
SQ SEQUENCE 901 AA; 102559 MW; 05840E7E9D257FAF CRC64;
MLIPSKLSRP VRLENTVLRE RLLARLTSAH HYRLALVTSP AGYGKTTLVS QWAAGKQNLG
WFSLDEGDNQ QERFAIYLIA AIQQATGGHC PTSEVMAQKR QYASLNSLFA QLFIELADWE
KPLYLVIDDY HLITNPVIHE AMRFFLRHQP ENVSLVVLSR NLPQLGIANL RVRDQLLEIG
SQQLAFNHQE AKQFFDCRLN APIEPAESSK MCDDVAGWAT ALQLIALSAR QNNTSAHQSA
RRLAGINASH LSDYLVDEVL DNIDVDVRMF LLKSALLRSM NDALIVRVTG EENGQMRLEE
IERQGLFLQR MDDNGEWFSY HPLFGNFLRQ RCQWELATQL PEIHRAAAEG WMAQGFPGEA
IHHALAAGDS AMLRDILLNH AWSLFNHSEL TLLEDSLKAL PWESLLANPK LVLLQAWLMQ
SQHRYGEVNT LLARAEQEMN GVMDDTLQGE FNALRAQVAI NHGDAQEAER LSIIALDTLP
LASFYSRIVA TSVHGEVLHC KGELSQSLAV MQQTEMMARR HDVWHYALWS LIQQSEILFA
QGFLQAAWET QDKAFTLIRE QHLEQLPLHE FLLRIRAQLL WAWARLDEAE TCARQGIDVL
ANYQPQQQLQ CLVLLVQCSL ARGALDNARS HLNRLENLLG NGPYHSDWVS NADKVRVIYW
QMTGDKAAAA NWLRQTPKPG SADNHFLQSQ WRNIARAQIL LGDFDPAEMV LEELNENARS
LRLMSDINRN LLLLNQLYWQ SGRKSDAQRV LLEALTLSNR TGFVSHFVIE GEAMAQQLRQ
LIQLNTLPEL EQHRAQLILR EINQHHRHKF AHFDEGFVNR LLTHPEVPEL IRTSPLTQRE
WQVLGLIYSG YSNEQIAGEL DVAATTIKTH IRNLYQKLGV AHRQAAVQHA QQLLKMMGYG
V
//
