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Database: UniProt
Entry: A0A2D0LFW8_9GAMM
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ID   A0A2D0LFW8_9GAMM        Unreviewed;       904 AA.
AC   A0A2D0LFW8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=Xkoz_00755 {ECO:0000313|EMBL:PHM74513.1};
OS   Xenorhabdus kozodoii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351676 {ECO:0000313|EMBL:PHM74513.1, ECO:0000313|Proteomes:UP000221101};
RN   [1] {ECO:0000313|EMBL:PHM74513.1, ECO:0000313|Proteomes:UP000221101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17907 {ECO:0000313|EMBL:PHM74513.1,
RC   ECO:0000313|Proteomes:UP000221101};
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:PHM74513.1}.
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DR   EMBL; NJCX01000004; PHM74513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0LFW8; -.
DR   OrthoDB; 1123107at2; -.
DR   Proteomes; UP000221101; 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:PHM74513.1};
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:PHM74513.1}.
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   904 AA;  104040 MW;  8BCD10A0543AC3A6 CRC64;
     MLIPSKLSRP LRLSNMVMRE RLLEKFNEIQ NYRLVLITSP AGYGKTTLMS QWAAGQEHLG
     WYSLDDSDNQ PERFASYLIA AIQQATQGHC VKSEVLAQKH QYASLPALIA QLFIELNEWQ
     KPIFLVIDDY HLIGNGLVHE AMRFFLRHQP ENLTLVVLSR HLPSLGIANL RVREQLLEID
     SHQLAFDYQE TQQFFAKRLA NPLEPEHCKQ LCNEVAGWAT ALQLIALSAR QSSNTTEISA
     KRLSGINASH LADYLVDEVL NRVDQATRDF LLHSSILRSM NDGLIACLTG EENGQQHLED
     IERQGLFIQR LDDSGEWFCF HPLFASFLRQ RCQWEMAAKL PELHRAAVKG WLMQGYPGEA
     IHHALAAGDT LLLRDILLQH AWELFNHSKL SLLEECMNAL PYELLLESPR LVLLQAWLAQ
     SQYRYYEVNA LLNQAEQSLK QKQIAIEPEL LAEFNALRAQ VAMNDGRPAD ADALAEKALA
     NLLPDNQYGR IVAMSVRGEV LHCNGQLASA LALMKQTEQL ARLCHSYHYA LWALLQQSEI
     LLAQGYLQAA YDTQSHAFDL IREQHLEQLP MHEFLLRLRS QLLWCWARID ESEEVARQGL
     DVLANYQPQQ QLQCLTQLAK CSLVRGDIDN ARRYLIRCEN LLSNGQYHRD WRTNTDELRV
     IIWQTLEDSS ALTQWLAQAE RPESFCNHFN QNQWRNIARV KILLDQYKEA ESILLKLNEY
     ARRLALVSDL NRNLLLCNLL YWQLGRKAEA QGVLIEALNL ANRTGFISHF VIEGELMALQ
     LRQLIQLNIL PEMEQHRAQR ILREINRQHR HKFAHFDETF VEQLLTHPDV PELIRNSPLT
     QREWQVLGLI YSGYSNDQIA AELEVAATTI KTHIRNLYQK MGIAHRQDAI SQAQKLMRMM
     GLGV
//
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