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Database: UniProt
Entry: A0A0U5L045_9GAMM
LinkDB: A0A0U5L045_9GAMM
Original site: A0A0U5L045_9GAMM 
ID   A0A0U5L045_9GAMM        Unreviewed;       907 AA.
AC   A0A0U5L045;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   11-DEC-2019, entry version 26.
DE   RecName: Full=HTH-type transcriptional regulator MalT {ECO:0000256|HAMAP-Rule:MF_01247, ECO:0000256|SAAS:SAAS00724615};
DE   AltName: Full=ATP-dependent transcriptional activator MalT {ECO:0000256|HAMAP-Rule:MF_01247};
GN   Name=malT {ECO:0000256|HAMAP-Rule:MF_01247,
GN   ECO:0000313|EMBL:CUU22539.1};
GN   ORFNames=EM595_0302 {ECO:0000313|EMBL:CUU22539.1};
OS   Erwinia gerundensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU22539.1, ECO:0000313|Proteomes:UP000059419};
RN   [1] {ECO:0000313|Proteomes:UP000059419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Blom J.;
RL   Submitted (NOV-2015) 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       ECO:0000256|SAAS:SAAS01071122}.
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, ECO:0000256|SAAS:SAAS01044130}.
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DR   EMBL; LN907827; CUU22539.1; -; Genomic_DNA.
DR   RefSeq; WP_067427208.1; NZ_LN907827.1.
DR   EnsemblBacteria; CUU22539; CUU22539; EM595_0302.
DR   KEGG; ege:EM595_0302; -.
DR   PATRIC; fig|1619313.3.peg.315; -.
DR   KO; K03556; -.
DR   OrthoDB; 1377603at2; -.
DR   BioCyc; GCF_001517405:G1EPQ-305-MONOMER; -.
DR   Proteomes; UP000059419; Chromosome 1.
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 {ECO:0000256|HAMAP-Rule:MF_01247, ECO:0000256|SAAS:SAAS00724627};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01247,
KW   ECO:0000256|SAAS:SAAS00724618};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01247,
KW   ECO:0000256|SAAS:SAAS00724617}; Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01247,
KW   ECO:0000256|SAAS:SAAS01008967};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01247,
KW   ECO:0000256|SAAS:SAAS00724612};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_01247,
KW   ECO:0000256|SAAS:SAAS00053185};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01247,
KW   ECO:0000256|SAAS:SAAS00053955}.
FT   DOMAIN          832..897
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50043"
FT   NP_BIND         39..46
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01247"
FT   COILED          707..727
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   907 AA;  103360 MW;  A46B14E617E8F16E CRC64;
     MLIPSKLSRP LRLQHTIIRE RLIARLAGTP NYRLALVASP AGYGKTTLVA QWASGKNDLG
     WFSLDESDNY PERFASYLMA AIQQATGNHC VRSEAMAQKR QYANLSALFS QLFIELATLD
     RPIYLVIDDY HLLTNEQIHQ AMRFFIRHQP ENLTLIVLSR NLPSLGIANL RVREQLLEIN
     SQSLAFTHDE ARQFFNCRLQ QPIDDGDSQR LCDEVAGWAT ALQLIALSER QSNTPTHQSA
     QRLSGINASH LSDYLVDEVL DCVDSSTRDF LLRSSVLRSM NESLIHRLTG EENAQLRLEE
     TERQGLFLQR MDDSGEWFKF HPLFASFLRQ RCQWELGGEL QHIHRAAAEG WMALGFANEA
     MHHALAADDK PLLRDILLNH AWSLFNHSEL ALLEEGLNAL SWEQRVETPR LILLQAWLAQ
     SQHRYSEVNM LLARAEEGMA QQHLAVDSVL SAEFDAIRAQ VAINAGQPNE AELLATKALA
     VLPLSSFYSR IVATSVKGEV LHCHGRLDEA MQMMMQTDQM ARQHDICHYA LWALLQQSEI
     LLAQGYLQSA FDTQEKAFQL VHDEGLTQLP MHEFLLRIRA QLLWSWAQLD QAEAAARQGL
     LVLENFHPQQ QLQCLAMLAK CALARGDLDN ARRHLIRCEN LLSNGQYHSD WVTNADKPRL
     IYWQMTDDKS AAASWLQQTR KPAQADNHFM QGQWRNIARA QILLGDYAAA EAVLDRLNES
     ARRLRLVSDL NRNLLLLNLL YWQTDRKTAA QQALIEALSL ANRTGFVSHF VIEGEAMAQQ
     LRQLLQLNAL PELEQHRANR ILRDINQHHR HKFAHFDEGF VHRLLTHPQV PELIRTSPLT
     QREWQVLGLI YSGYSNDQIA GELAVAQTTI KTHIRNLYQK LGVAHRQEAV QQAQQLLHLM
     GMSVSQA
//
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