ID MALT_YERPS Reviewed; 903 AA.
AC Q664J3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
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=YPTB3776;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX936398; CAH23014.1; -; Genomic_DNA.
DR RefSeq; WP_002208926.1; NZ_CP009712.1.
DR AlphaFoldDB; Q664J3; -.
DR SMR; Q664J3; -.
DR GeneID; 66843800; -.
DR KEGG; ypo:BZ17_2809; -.
DR KEGG; yps:YPTB3776; -.
DR PATRIC; fig|273123.14.peg.2948; -.
DR Proteomes; UP000001011; 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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd06170; LuxR_C_like; 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; 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_1000085787"
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
//
