ID A4XX16_PSEMY Unreviewed; 914 AA.
AC A4XX16;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=HTH-type transcriptional regulator MalT {ECO:0000256|HAMAP-Rule:MF_01247};
DE AltName: Full=ATP-dependent transcriptional activator MalT {ECO:0000256|HAMAP-Rule:MF_01247};
GN Name=malT {ECO:0000256|HAMAP-Rule:MF_01247};
GN OrderedLocusNames=Pmen_3129 {ECO:0000313|EMBL:ABP85882.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP85882.1};
RN [1] {ECO:0000313|EMBL:ABP85882.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP85882.1};
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., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-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:0000256|HAMAP-Rule:MF_01247}.
CC -!- ACTIVITY REGULATION: Activated by ATP and maltotriose, which are both
CC required for DNA binding. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01247}.
CC -!- SIMILARITY: Belongs to the MalT family. {ECO:0000256|HAMAP-
CC Rule:MF_01247}.
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DR EMBL; CP000680; ABP85882.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XX16; -.
DR STRING; 399739.Pmen_3129; -.
DR KEGG; pmy:Pmen_3129; -.
DR PATRIC; fig|399739.8.peg.3170; -.
DR eggNOG; COG2909; Bacteria.
DR HOGENOM; CLU_006325_3_0_6; -.
DR OrthoDB; 1123107at2; -.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_01247};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01247};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01247}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01247};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01247}; Transcription {ECO:0000256|HAMAP-Rule:MF_01247};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01247}.
FT DOMAIN 843..908
FT /note="HTH luxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50043"
FT COILED 789..818
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01247"
SQ SEQUENCE 914 AA; 103678 MW; C41986BEC8D40E45 CRC64;
MTTAARPPLP LIPAKLAAPS IHPGLLPRPR FDEWLQRLPQ VRLAVLQAPS GFGKTVLASQ
WAAAFAGAVA WLNLDGNDNS PRQFGRYLLN ALHRQLEGGC PQCVNRAEQG DDGLDGLLTR
LLAELPAEHP PLLLVLDEFE ALRNREVIAA LRFFLRNTPP WLTLLVCSRG LPDLGVAELR
VKRQLLALDA SHLAFELDEV QSLLELGLPI AINREQVERL NRRIGGWPCA LQLTLQEVQT
GRGMDLFLEA LQLGHPYVRD YFREQVLYGL DGATQDFLQS TCLLERFSAP LADRLTDSCN
GREMLETLER AGLFIQAVDP LRQWFAYHPL FASFLRNELS THHPQRMGEL HLRAAEALLE
EKMAEEAARH ALLAHDPQRV AQILETHGRH FYRQGRLELL QRCLAVLPES RVAESPLFTL
LQAWASQNQY QSDQVERWLQ AGEAVQREQF SAEQWQRIEG EYQAVRAQVA INQGDQQRAM
AFARQALALE PLTMRTSRVA ALSVLAESHF VQGDLAKAQH QHEENVRRAQ QINASHPVLW
SLGQLSEIAV AQGHLQKAYN LQERALQYIE QEKLPVTPIM EFIHRVRGQV LLEWHHLDAA
EQCALQGLEI LDTVGDHWFL QCYVLLARVA HARGQQSQCA DYIGRLKTLL AGDDYHIDWQ
ANAHAVMLTY WDSTQDKDSI RQWLATAPPL KPGANHFAQG NARNHVRAYL ALNQGDRALP
ILRQLQLDAE RHQLVMDQNR NHILQALAYW QREERQSSLD HLHQALTLAS GTGAIGSFLR
LGKPLIAMLK ALQHERRLDE LEHQRAERLI QLAQQQRDFS RAIRITLDEA VIQDIINRPD
VPELIRHSPL TRREWQVLSL IHAGLSNEQI SEHLNVAPTT IKTHIRSLYQ KLAITQRSEA
VQLARSLLSK IQGE
//
