ID   MALT_YERE8              Reviewed;         903 AA.
AC   A1JSF2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; OrderedLocusNames=YE3990;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL14010.1; -; Genomic_DNA.
DR   RefSeq; WP_011817355.1; NC_008800.1.
DR   RefSeq; YP_001008136.1; NC_008800.1.
DR   AlphaFoldDB; A1JSF2; -.
DR   SMR; A1JSF2; -.
DR   STRING; 393305.YE3990; -.
DR   EnsemblBacteria; CAL14010; CAL14010; YE3990.
DR   KEGG; yen:YE3990; -.
DR   PATRIC; fig|393305.7.peg.4248; -.
DR   eggNOG; COG2909; Bacteria.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   Proteomes; UP000000642; Chromosome.
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   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..903
FT                   /note="HTH-type transcriptional regulator MalT"
FT                   /id="PRO_1000085783"
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   903 AA;  103209 MW;  BFFE9677F9E7D450 CRC64;
     MLIPSKLSRP VRLQNTVIRD RLLVKLSGVA NYRLTLINCP AGYGKTTLIA QWAADQSDLG
     WYSLDESDNQ PERFATYLVA AIQLATGGHC SKSEAISQKH QYASLSALFA QLFIELSEWD
     GPLYLVIDDY HLITNDAIHE AMRFFLRHQP ENLTLIMLSR TLPPLGIANL RVRDQLLELG
     MQQLAFNHQE AQQFFDCRLS VPLEQGDSSR LCDEVEGWAT ALQLIALSSR QPNSSAQKSA
     KRLAGLNASH LSDYLVDEVL DQVDSDARAF LLRCSVLRSM NDALIVRLTG EDNGQQRLEE
     LERQGLFIHR MDDSGEWFCF HPLFATFLRQ RCQWEMALEL PELHHAAAEG WMALGYPAEA
     IHHALAAGDV GMLRDILLQH AWTLFNHSEL ALLEQCLVAL PYSLLVQNPE LALLQAWLAQ
     SQHRYGEVNT LLERAESAMQ ERKIPIDEIL RAEFDALRAQ VAINAGKPEE AEKLATDALK
     YLPMANFYSR IVATSVTGEV HHCKGELSRA LPMMQQTEQM ARRHEAYHYA LWALLQQSEI
     LIAQGFLQAA YETQDKAFDL IHEQHLEQLP MHEFLLRIRS QVLWSWSRLD EAEEAARKGI
     EILVNYQPQQ QLQCLAMLAK CSLARGDLDN ANMYIQRCEA LQHGSQYHLD WITNADKPRV
     IHWQMTGDKA AAANWLRQAE KPGMADNHFL QGQWRNIARI QIMLGRFNEA EVVLDELNEN
     ARRLRLTSDL NRNLLLSNIL YWQTERKSEA QKALIESLSL ANRTGFISHF VIEGEVMAQQ
     LRQLIQLNAL PELEQHRAQR ILKDINQHHR HKFAHFDEIF VDKLLTHPQV PELIRTSPLT
     QREWQVLGLI YSGYSNDQIA GELEVAATTI KTHIRNLYQK LGVAHRQDAV QQAQRLLQMM
     GYV