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P56255

- PCRA_GEOSE

UniProt

P56255 - PCRA_GEOSE

Protein

ATP-dependent DNA helicase PcrA

Gene

pcrA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    DNA helicase. Has a broad nucleotide specificity, even being able to hydrolyze ethenonucleotides, and is able to couple the hydrolysis to unwinding of DNA substrates. It is a 3'-5' helicase but at high protein concentrations it can also displace a substrate with a 5' tail. Preferred substrate being one with both single and double-stranded regions of DNA.

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei287 – 2871ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 166ATP1 PublicationPROSITE-ProRule annotation
    Nucleotide bindingi34 – 396ATP1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent DNA helicase activity Source: InterPro
    3. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA unwinding involved in DNA replication Source: InterPro

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent DNA helicase PcrA (EC:3.6.4.12)
    Gene namesi
    Name:pcrA
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 724724ATP-dependent DNA helicase PcrAPRO_0000102050Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    724
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Helixi14 – 218
    Beta strandi27 – 315
    Helixi37 – 5014
    Helixi56 – 583
    Beta strandi59 – 657
    Helixi66 – 8015
    Helixi81 – 844
    Beta strandi87 – 915
    Helixi92 – 10312
    Helixi104 – 1074
    Beta strandi114 – 1163
    Helixi118 – 13013
    Turni135 – 1384
    Helixi141 – 15313
    Helixi158 – 1614
    Helixi169 – 18618
    Beta strandi189 – 1913
    Helixi194 – 20512
    Helixi207 – 21610
    Beta strandi218 – 2247
    Helixi225 – 2273
    Helixi230 – 24011
    Turni241 – 2433
    Beta strandi246 – 2505
    Helixi252 – 2543
    Helixi258 – 2603
    Helixi265 – 2684
    Helixi270 – 2734
    Beta strandi278 – 2825
    Beta strandi286 – 2883
    Helixi290 – 30011
    Beta strandi304 – 3063
    Beta strandi312 – 3154
    Beta strandi321 – 3288
    Helixi329 – 34416
    Turni345 – 3473
    Helixi351 – 3533
    Beta strandi354 – 3607
    Helixi361 – 3633
    Helixi364 – 37310
    Beta strandi378 – 3814
    Helixi386 – 3883
    Helixi390 – 40314
    Helixi408 – 4147
    Beta strandi415 – 4184
    Turni421 – 4233
    Helixi424 – 43512
    Turni436 – 4383
    Turni442 – 4465
    Turni449 – 4513
    Turni454 – 4618
    Helixi462 – 47413
    Turni475 – 4773
    Helixi480 – 49011
    Helixi493 – 5008
    Helixi503 – 52523
    Helixi531 – 5377
    Turni538 – 5403
    Turni544 – 5463
    Beta strandi559 – 5635
    Helixi564 – 5674
    Beta strandi572 – 5776
    Turni584 – 5863
    Helixi588 – 5914
    Helixi594 – 60815
    Beta strandi611 – 62515
    Beta strandi628 – 6303
    Helixi636 – 6405
    Helixi643 – 6453
    Beta strandi646 – 6483

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PJRX-ray2.50A1-724[»]
    1QHGX-ray2.50A1-724[»]
    1QHHX-ray2.50A1-167[»]
    B168-440[»]
    C441-555[»]
    D556-724[»]
    2PJRX-ray2.90A/F1-548[»]
    B/G556-650[»]
    3PJRX-ray3.30A1-724[»]
    ProteinModelPortaliP56255.
    SMRiP56255. Positions 4-652.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56255.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 289280UvrD-like helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini290 – 569280UvrD-like helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the helicase family. UvrD subfamily.Curated
    Contains 1 uvrD-like helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 uvrD-like helicase C-terminal domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di1.10.10.160. 1 hit.
    3.40.50.300. 4 hits.
    InterProiIPR005751. ATP-dep_DNA_helicase_PcrA.
    IPR013986. DExx_box_DNA_helicase_dom.
    IPR014017. DNA_helicase_UvrD-like_C.
    IPR000212. DNA_helicase_UvrD/REP.
    IPR027417. P-loop_NTPase.
    IPR014016. UvrD-like_ATP-bd.
    [Graphical view]
    PANTHERiPTHR11070. PTHR11070. 1 hit.
    PfamiPF00580. UvrD-helicase. 1 hit.
    PF13361. UvrD_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01073. pcrA. 1 hit.
    PROSITEiPS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
    PS51217. UVRD_HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56255-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNFLSEQLLA HLNKEQQEAV RTTEGPLLIM AGAGSGKTRV LTHRIAYLMA    50
    EKHVAPWNIL AITFTNKAAR EMRERVQSLL GGAAEDVWIS TFHSMCVRIL 100
    RRDIDRIGIN RNFSILDPTD QLSVMKTILK EKNIDPKKFE PRTILGTISA 150
    AKNELLPPEQ FAKRASTYYE KVVSDVYQEY QQRLLRNHSL DFDDLIMTTI 200
    QLFDRVPDVL HYYQYKFQYI HIDEYQDTNR AQYTLVKKLA ERFQNICAVG 250
    DADQSIYRWR GADIQNILSF ERDYPNAKVI LLEQNYRSTK RILQAANEVI 300
    EHNVNRKPKR IWTENPEGKP ILYYEAMNEA DEAQFVAGRI REAVERGERR 350
    YRDFAVLYRT NAQSRVMEEM LLKANIPYQI VGGLKFYDRK EIKDILAYLR 400
    VIANPDDDLS LLRIINVPKR GIGASTIDKL VRYAADHELS LFEALGELEM 450
    IGLGAKAAGA LAAFRSQLEQ WTQLQEYVSV TELVEEVLDK SGYREMLKAE 500
    RTIEAQSRLE NLDEFLSVTK HFENVSDDKS LIAFLTDLAL ISDLDELDGT 550
    EQAAEGDAVM LMTLHAAKGL EFPVVFLIGM EEGIFPHNRS LEDDDEMEEE 600
    RRLAYVGITR AEEELVLTSA QMRTLFGNIQ MDPPSRFLNE IPAHLLETAS 650
    RRQAGASRPA VSRPQASGAV GSWKVGDRAN HRKWGIGTVV SVRGGGDDQE 700
    LDIAFPSPIG IKRLLAKFAP IEKV 724
    Length:724
    Mass (Da):82,488
    Last modified:July 15, 1998 - v1
    Checksum:i6D20CA468BFB4291
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PJR X-ray 2.50 A 1-724 [» ]
    1QHG X-ray 2.50 A 1-724 [» ]
    1QHH X-ray 2.50 A 1-167 [» ]
    B 168-440 [» ]
    C 441-555 [» ]
    D 556-724 [» ]
    2PJR X-ray 2.90 A/F 1-548 [» ]
    B/G 556-650 [» ]
    3PJR X-ray 3.30 A 1-724 [» ]
    ProteinModelPortali P56255.
    SMRi P56255. Positions 4-652.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P56255.

    Family and domain databases

    Gene3Di 1.10.10.160. 1 hit.
    3.40.50.300. 4 hits.
    InterProi IPR005751. ATP-dep_DNA_helicase_PcrA.
    IPR013986. DExx_box_DNA_helicase_dom.
    IPR014017. DNA_helicase_UvrD-like_C.
    IPR000212. DNA_helicase_UvrD/REP.
    IPR027417. P-loop_NTPase.
    IPR014016. UvrD-like_ATP-bd.
    [Graphical view ]
    PANTHERi PTHR11070. PTHR11070. 1 hit.
    Pfami PF00580. UvrD-helicase. 1 hit.
    PF13361. UvrD_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01073. pcrA. 1 hit.
    PROSITEi PS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
    PS51217. UVRD_HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterisation of Bacillus stearothermophilus PcrA helicase: evidence against an active rolling mechanism."
      Bird L.E., Brannigan J.A., Subramanya H.S., Wigley D.B.
      Nucleic Acids Res. 26:2686-2693(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
      Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
    3. "Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism."
      Velankar S.S., Soultanas P., Dillingham M.S., Subramanya H.S., Wigley D.B.
      Cell 97:75-84(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    4. "DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase."
      Soultanas P., Dillingham M.S., Velankar S.S., Wigley D.B.
      J. Mol. Biol. 290:137-148(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ATP.
    5. "Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation."
      Dillingham M.S., Soultanas P., Wigley D.B.
      Nucleic Acids Res. 27:3310-3317(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.

    Entry informationi

    Entry nameiPCRA_GEOSE
    AccessioniPrimary (citable) accession number: P56255
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 78 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

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3