Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23477

- ADDB_BACSU

UniProt

P23477 - ADDB_BACSU

Protein

ATP-dependent helicase/deoxyribonuclease subunit B

Gene

addB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent single-stranded exonuclease, acting in both directions. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' to 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.3 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Binds 1 4Fe-4S cluster.1 Publication
    Magnesium. At low magnesium concentrations there is no nuclease activity, but helicase activity is unaffected.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi801 – 8011Iron-sulfur (4Fe-4S)
    Metal bindingi1121 – 11211Iron-sulfur (4Fe-4S)
    Metal bindingi1124 – 11241Iron-sulfur (4Fe-4S)
    Metal bindingi1130 – 11301Iron-sulfur (4Fe-4S)

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi8 – 158ATPSequence Analysis

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. 5'-3' exonuclease activity Source: UniProtKB-HAMAP
    3. ATP binding Source: UniProtKB-HAMAP
    4. double-stranded DNA binding Source: UniProtKB-HAMAP
    5. helicase activity Source: UniProtKB-HAMAP
    6. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. double-strand break repair via homologous recombination Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU10620-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent helicase/deoxyribonuclease subunit B (EC:3.1.-.-, EC:3.6.4.12)
    Alternative name(s):
    ATP-dependent helicase/nuclease AddB
    Gene namesi
    Name:addB
    Ordered Locus Names:BSU10620
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU10620. [Micado]

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi801 – 8011C → A: Loss of iron-sulfur group binding, loss of DNA-binding. 1 Publication
    Mutagenesisi961 – 9611D → A: Some loss of nuclease activity, helicase and DNA-binding are unaltered; when associated with A-1172 in AddA nearly complete loss of nuclease activity. 1 Publication
    Mutagenesisi1121 – 11211C → A: Loss of iron-sulfur group binding, loss of DNA-binding. 1 Publication
    Mutagenesisi1124 – 11241C → A: Loss of iron-sulfur group binding, loss of DNA-binding. 1 Publication
    Mutagenesisi1130 – 11301C → A: Loss of iron-sulfur group binding, loss of DNA-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11661166ATP-dependent helicase/deoxyribonuclease subunit BPRO_0000064450Add
    BLAST

    Proteomic databases

    PaxDbiP23477.
    PRIDEiP23477.

    Interactioni

    Subunit structurei

    Heterodimer of AddA and AddB.2 Publications

    Protein-protein interaction databases

    DIPiDIP-60826N.
    IntActiP23477. 1 interaction.
    STRINGi224308.BSU10620.

    Structurei

    Secondary structure

    1
    1166
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi14 – 2815
    Beta strandi35 – 384
    Helixi41 – 433
    Helixi44 – 518
    Turni55 – 573
    Beta strandi58 – 669
    Helixi68 – 7912
    Helixi89 – 10214
    Helixi103 – 1064
    Turni110 – 1134
    Beta strandi114 – 1163
    Helixi118 – 13215
    Helixi137 – 1448
    Helixi155 – 17521
    Turni177 – 1793
    Helixi183 – 1853
    Helixi186 – 1938
    Turni194 – 1963
    Helixi198 – 2003
    Beta strandi204 – 2074
    Helixi215 – 22713
    Beta strandi229 – 2368
    Beta strandi242 – 2443
    Beta strandi248 – 2514
    Helixi253 – 26816
    Beta strandi273 – 2786
    Turni283 – 2864
    Helixi288 – 2958
    Beta strandi296 – 2983
    Beta strandi310 – 31910
    Helixi320 – 33617
    Helixi342 – 3443
    Beta strandi345 – 3506
    Helixi352 – 3543
    Helixi356 – 36510
    Beta strandi370 – 3745
    Helixi382 – 39514
    Helixi400 – 4078
    Turni408 – 4103
    Beta strandi411 – 4133
    Beta strandi415 – 4173
    Helixi419 – 43618
    Helixi441 – 4444
    Beta strandi445 – 4473
    Beta strandi457 – 4593
    Helixi465 – 49430
    Helixi498 – 51114
    Helixi514 – 52714
    Helixi531 – 55424
    Helixi562 – 57514
    Beta strandi584 – 5863
    Beta strandi588 – 5958
    Beta strandi602 – 6076
    Turni611 – 6166
    Beta strandi622 – 6243
    Helixi626 – 6349
    Helixi645 – 65814
    Beta strandi662 – 67211
    Beta strandi674 – 6763
    Helixi683 – 6919
    Beta strandi698 – 7003
    Helixi704 – 7063
    Helixi709 – 7124
    Helixi713 – 7153
    Helixi719 – 73416
    Helixi742 – 7509
    Helixi756 – 7638
    Turni764 – 7674
    Helixi777 – 7837
    Beta strandi786 – 7883
    Helixi792 – 8009
    Helixi802 – 8087
    Helixi824 – 84320
    Helixi848 – 8503
    Helixi853 – 86715
    Helixi868 – 8703
    Turni872 – 8743
    Helixi875 – 8784
    Helixi880 – 90425
    Beta strandi910 – 92415
    Beta strandi927 – 9315
    Turni932 – 9343
    Beta strandi935 – 95117
    Beta strandi954 – 96613
    Helixi971 – 9755
    Helixi981 – 99717
    Beta strandi1001 – 101010
    Helixi1024 – 103310
    Beta strandi1037 – 10426
    Helixi1045 – 10517
    Beta strandi1056 – 10594
    Beta strandi1061 – 10644
    Beta strandi1071 – 10733
    Helixi1082 – 110423
    Beta strandi1113 – 11153
    Helixi1121 – 11233
    Helixi1127 – 11304
    Beta strandi1134 – 11363
    Helixi1149 – 115911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3U44X-ray3.20B1-1166[»]
    3U4QX-ray2.80B1-1166[»]
    4CEHX-ray3.24B1-1166[»]
    4CEIX-ray2.80B1-1166[»]
    4CEJX-ray3.00B1-1166[»]
    ProteinModelPortaliP23477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 278278UvrD-like helicase ATP-bindingAdd
    BLAST
    Domaini281 – 586306UvrD-like helicase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3857.
    HOGENOMiHOG000285805.
    KOiK16899.
    OrthoDBiEOG6DC6FN.
    PhylomeDBiP23477.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_01452. AddB_type1.
    InterProiIPR014140. DNA_helicase_suAddB.
    IPR014017. DNA_helicase_UvrD-like_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF13361. UvrD_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR02773. addB_Gpos. 1 hit.
    PROSITEiPS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
    PS51217. UVRD_HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23477-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAEFLVGRS GSGKTKLIIN SIQDELRRAP FGKPIIFLVP DQMTFLMEYE     50
    LAKTPDMGGM IRAQVFSFSR LAWRVLQHTG GMSRPFLTST GVQMLLRKLI 100
    EEHKQEFKVY QKASDKSGFT AQVERMLTEF KRYCLEPEDI RRMAESGTAS 150
    EYRGERVLSE KLHDLSILYQ QMEKSLADQY LHSEDYLTLL AEHIPLAEDI 200
    KGAHIYVDGF YQFTPQEFRV LEQLMVHAEH ITFSLTADKP SYEREPHELE 250
    LFRMTGKTYY RLHQKAKELN LDITYKELSG TERHTKTPEL AHLEAQYEAR 300
    PAIPYAEKQE ALTVMQAANR RAELEGIARE IHALVREKGY RYKDVAILAR 350
    QPEDYKDMVK EVFADYEIPY FIDGKASMLN HPLIEFIRSS LDVLKGNWRY 400
    EAVFRCVKTE LLFPLNEPKA KVREQVDQLE NYCIAYGIKG DRWTKGDRFQ 450
    YRRFVSLDDD FAQTDQEIEM ENMLNDTRDW IVPPLFQLQK RMKKAKTVQE 500
    KAEALYRYLE ETDVPLKLDQ ERQRAEDDGR IIEAQQHQQA WDAVIQLLEE 550
    FVEMMGDDEI SLDLFQQMIE AGAESLTFSL IPPALDQVFV GNMDLSRMYG 600
    TSCTFVLGAN DGVLPARPDE NGVLSDDDRE WLKTIGVELS SGGRERLLDE 650
    HFLIYMAFSS PSDRLYVSYP IADAEGKTLL PSMIVKRLEE LFPHHKERLL 700
    TNEPEQVSDE EQLMYVVNKS VAQSFTASQL RLWTREYDIS DVWWSTYNVL 750
    MSEQDRLQSK KLFSSLFFRN EVKQLERSVS RQLYGERIQG SVSRMETFNA 800
    CPFSHFASHG LHLKERQFFK LEAPDIGQLF HSSLKLISDR LREQKLDWRD 850
    LTKEQCELFS YDAVERLAPK LQKEILLSSN RHYYVKEKLQ KIVTRVSGIL 900
    SEHAKASGFV PIGLELGFGG KGPLPPLTFQ LKNGCTMELV GRIDRVDKAE 950
    SSKGLLLRIV DYKSSDKGLD LAEVYYGLAL QMLTYLDLSI THSADWLGMR 1000
    ATPAGVLYFH IHDPMIQSNL PLGLDEIEQE IFKKFKMKGL LLGDQEVVRL 1050
    MDTTLQEGRS NIINAGLKKD GSLRSDSAAV GEKEFDLLTK HVRRTFQEAG 1100
    EQITDGRVSI EPYKMKNKTP CTYCAFKSVC QFDESLEENE YRPLKAEKDK 1150
    TILEWIKKEA DGNEHS 1166
    Length:1,166
    Mass (Da):134,645
    Last modified:June 16, 2009 - v2
    Checksum:iFA63593585A4CA73
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti843 – 8442EQ → DE in AAA22200. (PubMed:1646786)Curated
    Sequence conflicti843 – 8442EQ → DE in CAA74481. (PubMed:9579061)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63489 Genomic DNA. Translation: AAA22200.1.
    Y14081 Genomic DNA. Translation: CAA74481.1.
    AL009126 Genomic DNA. Translation: CAB12902.2.
    PIRiA39432.
    RefSeqiNP_388943.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12902; CAB12902; BSU10620.
    GeneIDi936341.
    KEGGibsu:BSU10620.
    PATRICi18973826. VBIBacSub10457_1107.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63489 Genomic DNA. Translation: AAA22200.1 .
    Y14081 Genomic DNA. Translation: CAA74481.1 .
    AL009126 Genomic DNA. Translation: CAB12902.2 .
    PIRi A39432.
    RefSeqi NP_388943.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3U44 X-ray 3.20 B 1-1166 [» ]
    3U4Q X-ray 2.80 B 1-1166 [» ]
    4CEH X-ray 3.24 B 1-1166 [» ]
    4CEI X-ray 2.80 B 1-1166 [» ]
    4CEJ X-ray 3.00 B 1-1166 [» ]
    ProteinModelPortali P23477.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60826N.
    IntActi P23477. 1 interaction.
    STRINGi 224308.BSU10620.

    Proteomic databases

    PaxDbi P23477.
    PRIDEi P23477.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12902 ; CAB12902 ; BSU10620 .
    GeneIDi 936341.
    KEGGi bsu:BSU10620.
    PATRICi 18973826. VBIBacSub10457_1107.

    Organism-specific databases

    GenoListi BSU10620. [Micado ]

    Phylogenomic databases

    eggNOGi COG3857.
    HOGENOMi HOG000285805.
    KOi K16899.
    OrthoDBi EOG6DC6FN.
    PhylomeDBi P23477.

    Enzyme and pathway databases

    BioCyci BSUB:BSU10620-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    HAMAPi MF_01452. AddB_type1.
    InterProi IPR014140. DNA_helicase_suAddB.
    IPR014017. DNA_helicase_UvrD-like_C.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF13361. UvrD_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR02773. addB_Gpos. 1 hit.
    PROSITEi PS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
    PS51217. UVRD_HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, and expression of Bacillus subtilis genes involved in ATP-dependent nuclease synthesis."
      Kooistra J., Venema G.
      J. Bacteriol. 173:3644-3655(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: OG1.
    2. "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
      Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
      Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "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.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 844.
    5. "The Bacillus subtilis addAB genes are fully functional in Escherichia coli."
      Kooistra J., Haijema B.J., Venema G.
      Mol. Microbiol. 7:915-923(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, FUNCTION IN E.COLI.
    6. "The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro."
      Chedin F., Ehrlich S.D., Kowalczykowski S.C.
      J. Mol. Biol. 298:7-20(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN EXONUCLEASE AND HELICASE, MAGNESIUM COFACTOR, ATP-DEPENDENCE.
    7. "Dynamic formation of RecA filaments at DNA double strand break repair centers in live cells."
      Kidane D., Graumann P.L.
      J. Cell Biol. 170:357-366(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECRUITS RECA TO DNA DOUBLE-STRAND BREAKS.
      Strain: 168 / YB886 / BG214.
    8. "Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the absence of DNA end processing."
      Sanchez H., Kidane D., Castillo Cozar M., Graumann P.L., Alonso J.C.
      J. Bacteriol. 188:353-360(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: 168 / YB886 / BG214.
    9. "A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases."
      Yeeles J.T.P., Dillingham M.S.
      J. Mol. Biol. 371:66-78(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-961.
    10. "An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases."
      Yeeles J.T.P., Cammack R., Dillingham M.S.
      J. Biol. Chem. 284:7746-7755(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, SUBUNIT, DNA-BINDING, MUTAGENESIS OF CYS-801; CYS-1121; CYS-1124 AND CYS-1130.

    Entry informationi

    Entry nameiADDB_BACSU
    AccessioniPrimary (citable) accession number: P23477
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This enzyme is a functional homolog of the RecBCD enzyme; unlike the RecBCD enzyme it degrades both duplex strands symmetrically.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3