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 08-MAY-2019, entry version 75.
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};
GN 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.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T.,
RA Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Challacombe J.F., Green L., Lindler L.E., Nikolich M.P.,
RA 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
CC regulon whose gene products are responsible for uptake and
CC catabolism of malto-oligosaccharides. Specifically binds to the
CC promoter region of its target genes, recognizing a short DNA motif
CC called the MalT box. {ECO:0000255|HAMAP-Rule:MF_01247}.
CC -!- ACTIVITY REGULATION: Activated by ATP and maltotriose, which are
CC both required for DNA binding. {ECO:0000255|HAMAP-Rule:MF_01247}.
CC -!- SUBUNIT: Monomer in solution. Oligomerizes to an active state in
CC the 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}.
DR EMBL; CP000950; ACA66473.1; -; Genomic_DNA.
DR RefSeq; WP_002208926.1; NZ_CP009792.1.
DR SMR; B1JHZ0; -.
DR EnsemblBacteria; ACA66473; ACA66473; YPK_0160.
DR KEGG; ypy:YPK_0160; -.
DR PATRIC; fig|502800.11.peg.767; -.
DR HOGENOM; HOG000218261; -.
DR KO; K03556; -.
DR OMA; SDWVSNA; -.
DR BioCyc; YPSE502800:G1GBB-162-MONOMER; -.
DR Proteomes; UP000000721; 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; Complete proteome;
KW DNA-binding; Nucleotide-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1 903 HTH-type transcriptional regulator MalT.
FT /FTId=PRO_1000139862.
FT DOMAIN 832 897 HTH luxR-type. {ECO:0000255|HAMAP-
FT Rule:MF_01247}.
FT NP_BIND 39 46 ATP. {ECO:0000255|HAMAP-Rule:MF_01247}.
FT DNA_BIND 856 875 H-T-H motif. {ECO:0000255|HAMAP-
FT 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
//
