ID I3D847_HAEPH Unreviewed; 901 AA.
AC I3D847;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
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:EIJ67890.1};
GN ORFNames=HMPREF1050_0549 {ECO:0000313|EMBL:EIJ67890.1};
OS Haemophilus parahaemolyticus HK385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ67890.1, ECO:0000313|Proteomes:UP000003016};
RN [1] {ECO:0000313|EMBL:EIJ67890.1, ECO:0000313|Proteomes:UP000003016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ67890.1,
RC ECO:0000313|Proteomes:UP000003016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
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:EIJ67890.1}.
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DR EMBL; AJSW01000053; EIJ67890.1; -; Genomic_DNA.
DR RefSeq; WP_005707304.1; NZ_UGHI01000002.1.
DR AlphaFoldDB; I3D847; -.
DR GeneID; 78223108; -.
DR PATRIC; fig|1095744.4.peg.1784; -.
DR OrthoDB; 1123107at2; -.
DR Proteomes; UP000003016; 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}; Transcription {ECO:0000256|HAMAP-Rule:MF_01247};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01247}.
FT DOMAIN 830..895
FT /note="HTH luxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50043"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01247"
SQ SEQUENCE 901 AA; 105205 MW; 4178E8047DE7542C CRC64;
MPALISGLMS SKFIAHFSKK ENKIERPALL AKLEKAKNYP LTLLAAPAGY GKTTLMAEWQ
AIQTAKHQRV SWLSLDKSDN QAVEFARYFT QALRDATHLS FSHCLFQDDL TRYFHELLLE
LQSIRSPFYL ILDDYHLIEN AEIHEAIRFW LKHQPEMMHL ILLSRTLPPI SITQLRLREK
LLEIGVNDLA FDLEQSRQLI EQATHITLSE TALHLLYEHT QGWISALQLL CFSLKTSLEW
LNTPEKLFAS LSQQYIEDYL SEEVFHFIPS QTQYFMQCCA LLHKMNERLV FALTQAENGI
YQLAELEKQG LFVQRNIHEN GETWWQFHPI LSDFLRQRCR MEHPQTWRTL HHLAITEWLK
LGNGTEALYH AQILEEPALL YKVLQEYGWK LFHQGQLKLL EECLNLMPAE QIWQDSNLVL
LKAWLSQSQH RYQEVSGILQ NFKPNQPLEE DLQAHFEALQ AQVAINEGNE DLAYQLANRA
LVHFSSKVGY AQIVANSIIG EAQHCQGYLK EGLQRMQKVE KMALEHSAYH QWLWSKLQQA
EMLSAQGFLQ SAYDLLKDTT QQAQLLHKIP MHEFLFRLRG QILWEWHHLD EAEEMANAGI
EVLEKESEQA HCLALIAKIS LTKGNLTNAS RLIEQGKNLL ASHSVHRDWL TTFDEVQLYY
WQISEEKAPL EGWLAQTTFP TQDHNHFLQR QWRNIARCYL LQAQFDKALE IVNRLLKTTA
IFNLISDTQR ALILRNRIYY QQDQYDLAQR DLIQALNLSQ QTNFISAFVI EGELMAEQIR
QLLQINVLDD LSTHKAKFIL RSINQHHRHK FAHFDEEFVS HLLKNPQLPE LLKISPLTSR
EWQVLGLIYA GYSNEQISQE LVVAITTIKT HIRNLYQKIG VENRIEAIEY TKSLLKMMGY
N
//
