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Database: UniProt
Entry: A0A2D0KMX7_9GAMM
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ID   A0A2D0KMX7_9GAMM        Unreviewed;       905 AA.
AC   A0A2D0KMX7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=Xsto_02672 {ECO:0000313|EMBL:PHM64789.1};
OS   Xenorhabdus stockiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM64789.1, ECO:0000313|Proteomes:UP000222366};
RN   [1] {ECO:0000313|EMBL:PHM64789.1, ECO:0000313|Proteomes:UP000222366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM64789.1,
RC   ECO:0000313|Proteomes:UP000222366};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
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:PHM64789.1}.
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DR   EMBL; NJAJ01000024; PHM64789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0KMX7; -.
DR   Proteomes; UP000222366; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; 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}; Kinase {ECO:0000313|EMBL:PHM64789.1};
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};
KW   Transferase {ECO:0000313|EMBL:PHM64789.1}.
FT   DOMAIN          832..897
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   905 AA;  104390 MW;  F97C915FFD8D5278 CRC64;
     MLIPSKLSRP LRLNHMVMRE RLLAQLNEAQ NYRLVLVTSP AGYGKTTLMS QWSAGQGNLG
     WYSLDDSDNQ PERFASYLIA AIQQATQGHC VKSEVLAQKH QYANLSALFA QLFIELNEWK
     QSLFLVIDDY HLIVNNLIHE AMRFFLRHQP ENLTLIILSR QLPSLGVANL RVREQLLEFD
     SQQLAFNYQE AQQFFDKRLP SPLDADNCRQ LCHDVAGWAT ALQLIALSAR QAGNTAEISA
     KRLSGINAGH LSDYLVDEVL NRVDQGTREF LLRSSILRSM NDGLIVCLTG MENGQQRLED
     IERQGLFIQR MDDFGEWFCF HPLFATFLRQ RCHWEMASDL PKLHSMAAEG WLRQGYPGEA
     IHHALAAGDT KLLCDILLQY AWELFNQSQL SLLEECMNAL PYEQLLEKPR LVLLQAWLAQ
     SQHRHYEVNA LLNQAEQSLK QKQITIEAEL LGEFDALRAQ VAINDGRPDD ADLLAEKALA
     ALLPDNEYGR IVAMSVKGEV LHCKGALSQA LALMKQTEQL ARRCHVYHYA LWALLQQSEI
     LLAQGYLQGA YETQKHAFDL VREQHMEQLP MHEFLLRIRS QLLWCWARID ESEEAARHGL
     EVLSNFQPQQ QLQCLSQLVK CSLIRGDIDN ARRHLTRCEN LLSNGHYHRD WRTNTDKLRI
     IIWQHLEDHI SVAQWLAQAE KPESFSNHFN QNQWRNIARA QILLGQYEEA ESILNMLNQY
     AVKLELVSDL NRNLLLCNLL HWQLGRKAEA QQVLIEALKL ANRTGFISHF VLEGELMALQ
     LRQLIQLNIL PDFEQHRAQR ILREINRQHR HKFAHFDETF VEQLITHPDV PELIRNSPLT
     QREWQVLGLI YSGYSNEQIA TELEVAATTI KTHIRNLYQK MGITHRQEAI QQAQNLMKMM
     GLGVQ
//
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