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MALT_VIBPA
ID   MALT_VIBPA              Reviewed;         902 AA.
AC   Q87FQ5;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=VPA1623;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000032; BAC62966.1; -; Genomic_DNA.
DR   RefSeq; NP_801133.1; NC_004605.1.
DR   RefSeq; WP_005480178.1; NC_004605.1.
DR   AlphaFoldDB; Q87FQ5; -.
DR   SMR; Q87FQ5; -.
DR   STRING; 223926.28810025; -.
DR   EnsemblBacteria; BAC62966; BAC62966; BAC62966.
DR   GeneID; 1192319; -.
DR   KEGG; vpa:VPA1623; -.
DR   PATRIC; fig|223926.6.peg.4542; -.
DR   eggNOG; COG2909; Bacteria.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   Proteomes; UP000002493; Chromosome 2.
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   Gene3D; 3.40.50.300; -; 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; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..902
FT                   /note="HTH-type transcriptional regulator MalT"
FT                   /id="PRO_0000184170"
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   902 AA;  104077 MW;  CA9DFC17CA0E486D CRC64;
     MWIPSKLTRP GRLHNAIVRP RVLDLLQQAP YYKLVLFRSP AGYGKTTMAA QWLSDKPNVG
     WYSIDDSDND GFRFVNYLLQ ALNKATNFSC SNAQKLAEKR QISSLRSLFS EVFAEMADFH
     QECYVVLDDY HLITNDEIHE SMRFFLKHMP DNLTVVVTSR AAPPLGTANL RVRDLMIEIG
     NEMLAFDTEE TTRFFNQRIA DGIDEDMANS LRTYVEGWPS AMQLIALQAQ HQNRTLAQTV
     ESVSQFNHAH LWDYLVEEVF DLLDHETRHF LMQVSVLDHF NDELVFALTQ REDALGLIES
     LNRYGLFIYP LEGEHNWFRF HNLFGEFLSH ERQARIPQQE KDLHRNAAVA WLQQKSPHQA
     IHHAQKSNDK DLVVEILNEF GWKMFNQGEL STLEHAINKL DAELLFSHPK LTMLRAWLAQ
     SQHRYNQVGQ LLEEAEEEHK KRNIELDIHY QGQANALLAQ VAINSNQPEK ALELAELALS
     QLDNTIYRSR IVATSVVGEV NHVLGKLDRA LPMMQQTEKL ARQYQVYHQA LWAILQQSEI
     LIAQGYVQAA FELQDSGFRL IEDQQLQHVP LHEFLLRIRA QVLWCWNRLD EAEECAYRGL
     QILENHSPSK HLHSYSMLAR IAIGRGELDK AGKFIEHIQH LMKQSTYHVD WTANASLSLI
     LFWQARGNTE AMQEWLNTAV RPESACNHFL QLQWRNIVRA HINLGQYEEA RQALNFLQSE
     ARRTNLITDT NRNLVVEAVL AARQKDEEQA KALLKEALVM TNQTGMVGNF LIDGATIGGL
     LEKLSLRHEL GDLERHRAQQ LMKDISSNQR SRSIHFDEDF IEKLVNHPNV PELVRTSPLT
     QREWQVLGLI YSGFSNEQIA QELDVAGTTI KTHIRNLYQK LNIANRKEAI VTAENLLQLM
     GY
 
 
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