ID   MALT_YERPY              Reviewed;         903 AA.
AC   B1JHZ0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=YPK_0160;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) 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: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; CP000950; ACA66473.1; -; Genomic_DNA.
DR   RefSeq; WP_002208926.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JHZ0; -.
DR   SMR; B1JHZ0; -.
DR   PRIDE; B1JHZ0; -.
DR   EnsemblBacteria; ACA66473; ACA66473; YPK_0160.
DR   GeneID; 66843800; -.
DR   KEGG; ypy:YPK_0160; -.
DR   PATRIC; fig|502800.11.peg.767; -.
DR   OMA; SDWVSNA; -.
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_1000139862"
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;  103165 MW;  728A538719E42251 CRC64;
     MLIPSKLSRP VRLQNTVVRD RLLVKLSSAA NYRLTLINCP AGYGKTTLIA QWAADQSNLG
     WYSLDESDNQ SERFATYLIA AIQLATGGHC SKSEALSQKH QYANLSALFS QLFIELSNWD
     GPLYLVIDDY HLITNDAIHE AMRFFLRHQP ENLTLIILSR TLPSLGIANL RVRDQLLELG
     MQQLAFNHHE AQQFFECRLS SPLEQGDSSR LCDEVEGWVT ALQLIALSSR QPNSSAQKSA
     KRLAGLNASH LSDYLVDEVL DQVDSKARAF LLRCSVLRSM NDALIVRLTG EDNGQQLLEE
     LERQGLFIHR MDDSAEWFCF HPLFATFLRQ RCQWELALEL PELHHAAAEG WMALGYPAEA
     IHHALAAGDV GMLRDILLQH AWSLFHHSEL ALLEQCLTAL PYPLLVQNPE LALLQAWLAQ
     SQHRYSEVNT LLEQAELAMQ ERKIPVDEIL RAEFGALRAQ VAINAGKPDE AEKLATDALK
     YLPMAHYYSR IVATSVTGEV HHCKGELARA LPMMQQTEQM ARRHEAYHYA LWALLQQSEI
     LIAQGFLQAA YETQEKAFEL IREQHLEQLP MHEFLLRIRS QVLWSWSRLD EAEEAARKGV
     EILANYQPQQ QLQCLAMLAK CSLARGDLDN ANVYIQRCEA LQHGSQYHLD WITNADKPRV
     IHWQMTGDKV AAASWLRQTE KPGMADNHFL QGQWRNIARV QIILGRFDEA EVVLDELNEN
     ARRLRLTSDL NRNLLLSNTL YWQTERKGEA QKALIESLTL ANRTGFISHF VIEGEAMAQQ
     LRQLIQLNAL PELEQHRAQR ILKDINQHHR HKFAHFDEIF VDKLLTHPQV PELIRTSPLT
     QREWQVLGLI YSGYSNDQIA NELDVAATTI KTHIRNLYQK LGVAHRQEAV QQAQRLLQMM
     GYV