ID   MALT_SERP5              Reviewed;         904 AA.
AC   A8GKU0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Spro_4637;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV43730.1; -; Genomic_DNA.
DR   RefSeq; WP_012147312.1; NC_009832.1.
DR   AlphaFoldDB; A8GKU0; -.
DR   SMR; A8GKU0; -.
DR   STRING; 399741.Spro_4637; -.
DR   EnsemblBacteria; ABV43730; ABV43730; Spro_4637.
DR   KEGG; spe:Spro_4637; -.
DR   eggNOG; COG2909; Bacteria.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   OrthoDB; 1377603at2; -.
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..904
FT                   /note="HTH-type transcriptional regulator MalT"
FT                   /id="PRO_1000085778"
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   904 AA;  103392 MW;  1E0AC421AE3BB3EE CRC64;
     MLIPSKLSRP VRLQNTVIRD RLLAKLASTA NYRLTLVNCP AGYGKTTLVA QWAAGKSDLG
     WYSLDESDNQ PERFASYLIA ALQLASGGHC VKSEALSQKH QYASLSALFA QLFIELSDWH
     QPLYLVIDDY HLITNDVIHE AMRFFLRHQP ENLTLILLSR TLPPLGIANL RVRDQLLEMG
     TQQLAFTHQE AKQFFDCRLV SPMESQDSSR LCDEVEGWAT ALQLIALSAR QSNSSAQQSA
     KRLAGLNASH LSDYLVDEVL DHVDAEARAF LLRCSVLRSM NDALIVRLTG EDNGQQRLEE
     LERQGLFIHR MDDSGEWFCF HPLFATFLRQ RCQWELALEL PGLHRAAAEG WLALGYPAEA
     IHHALAASDV SMLRDILLQH AWSLFHHSEL ALLEECLNAL PYERLIQNPK LALLQAWLAQ
     SQHRYSEVNT LLERAEQAMR DQKIEVDRTL EAEFDALRAQ VAINAGKPEE AERLATEALK
     FLPLSSYYSR IVATSVTGEV HHCKGELARA LPMMQQTEQM ARRHQAYHYA LWALLQQSEI
     LIAQGFLQAA FETQDKAFEL VREQHLEQLP MHEFLLRIRS QILWSWSRLD EAEDAAREGL
     KILANYQPQQ QLQCIAMLAK CSLARGDLDN ANAHMQRCEV LLHGTQYHRD WLTNADKPRV
     IHWQMTGDTT AAAQWLRQTE KPGMADNHFM QGQWRNIARV QIMLGQYEEA EVVLDELNEN
     ARRLRLVSDL NRNLLLSNQL YWQMERKSDA QKVLMEALSL ASRTGFISHF VIEGEAMAQQ
     LRQLIQLNTL PELENHRAQR ILRDINQHHR HKFAHFDENF VDKLLTHPQV PELIRTSPLT
     QREWQVLGLI YSGYSNDQIA GELAVAATTI KTHIRNLYQK LGVAHRQEAV QQAQQLLKMM
     GYGA