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O32138

- PUCR_BACSU

UniProt

O32138 - PUCR_BACSU

Protein

Purine catabolism regulatory protein

Gene

pucR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Activates the expression of pucFG, pucH, pucI, pucJKLM and guaD, while it represses pucABCDE and its own expression.2 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. purine nucleobase metabolic process Source: UniProtKB-KW
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Purine metabolism, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU32420-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Purine catabolism regulatory protein
    Gene namesi
    Name:pucR
    Synonyms:yunI
    Ordered Locus Names:BSU32420
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU32420. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Purine catabolism regulatory proteinPRO_0000165945Add
    BLAST

    Proteomic databases

    PaxDbiO32138.

    Expressioni

    Inductioni

    Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression slightly decreases when allantoin is added during limiting-nitrogen conditions.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU32420.

    Structurei

    3D structure databases

    ProteinModelPortaliO32138.
    SMRiO32138. Positions 470-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CdaR family.Curated

    Phylogenomic databases

    eggNOGiCOG2508.
    HOGENOMiHOG000009087.
    KOiK09684.
    OMAiRNEPVYI.
    OrthoDBiEOG6038SW.
    PhylomeDBiO32138.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR009057. Homeodomain-like.
    IPR025736. PucR_C-HTH_dom.
    IPR012914. PucR_dom.
    [Graphical view]
    PfamiPF13556. HTH_30. 1 hit.
    PF07905. PucR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O32138-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNILDVMKIP AFENANLIAG KAGGEREVQH VNMMDAPDIV DFLHKNELLV    50
    TTAYHLKDHP HQLSELIRQM AKRGCAGLGI KTKRYLEDIP KEIIELADSY 100
    AFPIIELPEH IRLGDIVNAT LSHILDMRSN ELQQAIYAHK KFTNHIMSGK 150
    GLQSLLKKVS DILQLPVLLL DQHAKMLSAS HQISVETEKL KGTLNTVSGP 200
    FFTCFSTISD QKTYSVLPIY NHEKNCGYLL IPDMVQAGDK GLILTIEQAA 250
    NVISFELLKE NALKQFSRRA RNEFFNNFIE RTFSSDDEIK NRAKEFKLRW 300
    DQKYMCIAGK LDRNDESISF TENQLASDSV FEFLEGELSA FPFPPHFFMK 350
    GNVGIILIEA TDSWSEMHAS VISFLEQFQT QVSAQFKRTV SFGISNICQK 400
    LIDVPDAFTE ASDALQSGHL SRSTAFIQVY HAKDVPELLR LLPVEDLKKF 450
    YNSTLQSLAE KQQEDQSLLH TLSVYLETHC QISETAKRLY VHRNTVIYRL 500
    EKCEELLGKS LKDPETTMRL RLALRMQRLI S 531
    Length:531
    Mass (Da):60,514
    Last modified:January 1, 1998 - v1
    Checksum:iCC2DA7F96247452F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15232.1.
    PIRiD70016.
    RefSeqiNP_391122.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15232; CAB15232; BSU32420.
    GeneIDi937221.
    KEGGibsu:BSU32420.
    PATRICi18978456. VBIBacSub10457_3391.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15232.1 .
    PIRi D70016.
    RefSeqi NP_391122.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O32138.
    SMRi O32138. Positions 470-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU32420.

    Proteomic databases

    PaxDbi O32138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15232 ; CAB15232 ; BSU32420 .
    GeneIDi 937221.
    KEGGi bsu:BSU32420.
    PATRICi 18978456. VBIBacSub10457_3391.

    Organism-specific databases

    GenoListi BSU32420. [Micado ]

    Phylogenomic databases

    eggNOGi COG2508.
    HOGENOMi HOG000009087.
    KOi K09684.
    OMAi RNEPVYI.
    OrthoDBi EOG6038SW.
    PhylomeDBi O32138.

    Enzyme and pathway databases

    BioCyci BSUB:BSU32420-MONOMER.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR009057. Homeodomain-like.
    IPR025736. PucR_C-HTH_dom.
    IPR012914. PucR_dom.
    [Graphical view ]
    Pfami PF13556. HTH_30. 1 hit.
    PF07905. PucR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
      Schultz A.C., Nygaard P., Saxild H.H.
      J. Bacteriol. 183:3293-3302(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168.
    3. "Transcription analysis of the Bacillus subtilis PucR regulon and identification of a cis-acting sequence required for PucR-regulated expression of genes involved in purine catabolism."
      Beier L., Nygaard P., Jarmer H., Saxild H.H.
      J. Bacteriol. 184:3232-3241(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168.

    Entry informationi

    Entry nameiPUCR_BACSU
    AccessioniPrimary (citable) accession number: O32138
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3