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)

P23478

- ADDA_BACSU

UniProt

P23478 - ADDA_BACSU

Protein

ATP-dependent helicase/nuclease subunit A

Gene

addA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. 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' -> 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 AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.3 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Magnesium. At low magnesium concentrations there is no nuclease activity, but helicase activity is unaffected.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 378ATPSequence Analysis

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-HAMAP
    3. ATP-dependent DNA helicase activity Source: UniProtKB-HAMAP
    4. double-stranded DNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

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

    Keywords - Molecular functioni

    Exonuclease, Helicase, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU10630-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent helicase/nuclease subunit A (EC:3.1.-.-, EC:3.6.4.12)
    Alternative name(s):
    ATP-dependent helicase/nuclease AddA
    Gene namesi
    Name:addA
    Ordered Locus Names:BSU10630
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU10630. [Micado]

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361K → A: Loss of helicase and nuclease activity. DNA-binding is unaltered. 1 Publication
    Mutagenesisi1172 – 11721D → A: Some loss of nuclease activity, helicase and DNA-binding are unaltered. No production of chi fragments; when associated with A-961 in AddB nearly complete loss of nuclease activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12321232ATP-dependent helicase/nuclease subunit APRO_0000064449Add
    BLAST

    Proteomic databases

    PaxDbiP23478.

    Interactioni

    Subunit structurei

    Heterodimer of AddA and AddB.2 Publications

    Protein-protein interaction databases

    DIPiDIP-60825N.
    STRINGi224308.BSU10630.

    Structurei

    Secondary structure

    1
    1232
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 113
    Helixi13 – 208
    Beta strandi26 – 305
    Helixi36 – 4813
    Beta strandi51 – 533
    Helixi57 – 593
    Beta strandi60 – 634
    Helixi67 – 8721
    Helixi92 – 1009
    Turni101 – 1033
    Beta strandi104 – 1074
    Helixi109 – 12012
    Helixi121 – 1233
    Helixi135 – 15622
    Helixi159 – 16810
    Helixi175 – 18814
    Beta strandi191 – 1933
    Helixi194 – 1996
    Helixi202 – 2054
    Turni213 – 2153
    Helixi219 – 24325
    Beta strandi246 – 2494
    Helixi256 – 26914
    Turni270 – 2723
    Helixi274 – 28310
    Beta strandi294 – 2974
    Helixi299 – 3046
    Helixi307 – 32317
    Beta strandi324 – 3263
    Helixi328 – 36235
    Helixi368 – 37912
    Beta strandi380 – 3845
    Beta strandi387 – 3904
    Helixi392 – 4009
    Beta strandi402 – 4087
    Helixi409 – 4113
    Helixi414 – 42310
    Helixi428 – 4303
    Beta strandi433 – 4375
    Helixi439 – 4413
    Turni445 – 4484
    Helixi452 – 4609
    Beta strandi461 – 4644
    Beta strandi466 – 4683
    Beta strandi470 – 4745
    Beta strandi476 – 4805
    Helixi482 – 49312
    Helixi498 – 5014
    Turni507 – 5093
    Beta strandi524 – 5307
    Helixi546 – 56318
    Beta strandi568 – 5714
    Helixi572 – 5743
    Beta strandi576 – 5794
    Helixi582 – 5843
    Beta strandi585 – 59410
    Helixi595 – 60410
    Beta strandi605 – 6073
    Beta strandi609 – 6113
    Beta strandi614 – 6163
    Helixi617 – 6193
    Helixi621 – 63414
    Helixi639 – 6479
    Turni649 – 6513
    Helixi655 – 6628
    Beta strandi666 – 6683
    Helixi670 – 68011
    Helixi686 – 70722
    Helixi710 – 72112
    Helixi723 – 7275
    Helixi733 – 75018
    Turni752 – 7543
    Helixi758 – 77013
    Beta strandi783 – 7864
    Beta strandi788 – 7925
    Helixi793 – 7953
    Turni796 – 7983
    Beta strandi801 – 8077
    Helixi816 – 8194
    Beta strandi820 – 8256
    Turni826 – 8283
    Beta strandi829 – 8324
    Beta strandi834 – 8363
    Turni837 – 8404
    Beta strandi841 – 8433
    Helixi846 – 87227
    Beta strandi874 – 88310
    Helixi887 – 89711
    Beta strandi901 – 9044
    Turni907 – 9115
    Helixi917 – 9259
    Beta strandi926 – 9283
    Helixi940 – 9445
    Beta strandi949 – 9546
    Helixi956 – 9594
    Helixi973 – 9786
    Helixi991 – 9999
    Helixi1005 – 10073
    Beta strandi1010 – 10167
    Turni1048 – 10503
    Helixi1057 – 106812
    Helixi1079 – 109113
    Helixi1097 – 11026
    Helixi1105 – 11095
    Helixi1110 – 11134
    Helixi1115 – 11217
    Beta strandi1124 – 113714
    Helixi1138 – 11403
    Beta strandi1147 – 11493
    Beta strandi1151 – 116313
    Beta strandi1168 – 11747
    Turni1183 – 11853
    Turni1187 – 11893
    Helixi1190 – 11967
    Helixi1198 – 121215
    Beta strandi1216 – 12238
    Turni1224 – 12274
    Beta strandi1228 – 12314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3U44X-ray3.20A1-1232[»]
    3U4QX-ray2.80A1-1232[»]
    4CEHX-ray3.24A1-1232[»]
    4CEIX-ray2.80A1-1232[»]
    4CEJX-ray3.00A1-1232[»]
    ProteinModelPortaliP23478.
    SMRiP23478. Positions 11-79.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 481473UvrD-like helicase ATP-bindingAdd
    BLAST
    Domaini508 – 798291UvrD-like helicase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the helicase family. AddA subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG1074.
    HOGENOMiHOG000015621.
    KOiK16898.
    OrthoDBiEOG6HJ22G.
    PhylomeDBiP23478.

    Family and domain databases

    Gene3Di3.40.50.300. 4 hits.
    3.90.320.10. 1 hit.
    HAMAPiMF_01451. AddA.
    InterProiIPR014152. DNA_helicase_suAddA.
    IPR014017. DNA_helicase_UvrD-like_C.
    IPR000212. DNA_helicase_UvrD/REP.
    IPR011604. Exonuc_phg/RecB_C.
    IPR027417. P-loop_NTPase.
    IPR011335. Restrct_endonuc-II-like.
    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. 3 hits.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsiTIGR02785. addA_Gpos. 1 hit.
    PROSITEiPS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
    PS51217. UVRD_HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23478-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIPKPADST WTDDQWNAIV STGQDILVAA AAGSGKTAVL VERMIRKITA     50
    EENPIDVDRL LVVTFTNASA AEMKHRIAEA LEKELVQRPG SLHIRRQLSL 100
    LNRASISTLH SFCLQVLKKY YYLIDLDPGF RIADQTEGEL IGDEVLDELF 150
    EDEYAKGEKA FFELVDRYTT DRHDLDLQFL VKQVYEYSRS HPNPEAWLES 200
    FVHLYDVSEK SAIEELPFYQ YVKEDIAMVL NGAKEKLLRA LELTKAPGGP 250
    APRADNFLDD LAQIDELIQH QDDFSELYKR VPAVSFKRAK AVKGDEFDPA 300
    LLDEATDLRN GAKKLLEKLK TDYFTRSPEQ HLKSLAEMKP VIETLVQLVI 350
    SYGKRFEAAK QEKSIIDFSD LEHYCLAILT AENDKGEREP SEAARFYQEQ 400
    FHEVLVDEYQ DTNLVQESIL QLVTSGPEET GNLFMVGDVK QSIYRFRLAE 450
    PLLFLSKYKR FTESGEGTGR KIDLNKNFRS RADILDSTNF LFKQLMGGKI 500
    GEVDYDEQAE LKLGAAYPDN DETETELLLI DNAEDTDASE EAEELETVQF 550
    EAKAIAKEIR KLISSPFKVY DGKKKTHRNI QYRDIVILLR SMPWAPQIME 600
    ELRAQGIPVY ANLTSGYFEA VEVAVALSVL KVIDNPYQDI PLASVLRSPI 650
    VGADENELSL IRLENKKAPY YEAMKDYLAA GDRSDELYQK LNTFYGHLQK 700
    WRAFSKNHSV SELIWEVYRD TKYMDYVGGM PGGKQRQANL RVLYDRARQY 750
    ESTAFRGLFR FLRFIERMQE RGDDLGTARA LSEQEDVVRL MTIHSSKGLE 800
    FPVVFVAGLG RNFNMMDLNK SYLLDKELGF GTKYIHPQLR ISYPTLPLIA 850
    MKKKMRRELL SEELRVLYVA LTRAKEKLFL IGSCKDHQKQ LAKWQASASQ 900
    TDWLLPEFDR YQARTYLDFI GPALARHRDL GDLAGVPAHA DISGHPARFA 950
    VQMIHSYDLL DDDLEERMEE KSERLEAIRR GEPVPGSFAF DEKAREQLSW 1000
    TYPHQEVTQI RTKQSVSEIK RKREYEDEYS GRAPVKPADG SILYRRPAFM 1050
    MKKGLTAAEK GTAMHTVMQH IPLSHVPSIE EAEQTVHRLY EKELLTEEQK 1100
    DAIDIEEIVQ FFHTEIGGQL IGAKWKDREI PFSLALPAKE IYPDAHEADE 1150
    PLLVQGIIDC LYETEDGLYL LDYKSDRIEG KFQHGFEGAA PILKKRYETQ 1200
    IQLYTKAVEQ IAKTKVKGCA LYFFDGGHIL TL 1232
    Length:1,232
    Mass (Da):141,087
    Last modified:June 16, 2009 - v2
    Checksum:i2A1B70FA4E645FE4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti780 – 7801A → G in AAA22201. (PubMed:1646786)Curated
    Sequence conflicti780 – 7801A → G in CAA74482. (PubMed:9579061)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63489 Genomic DNA. Translation: AAA22201.1.
    Y14081 Genomic DNA. Translation: CAA74482.1.
    AL009126 Genomic DNA. Translation: CAB12903.2.
    Y09476 Genomic DNA. Translation: CAA70668.1.
    PIRiB39432.
    RefSeqiNP_388944.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12903; CAB12903; BSU10630.
    GeneIDi939793.
    KEGGibsu:BSU10630.
    PATRICi18973828. VBIBacSub10457_1108.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63489 Genomic DNA. Translation: AAA22201.1 .
    Y14081 Genomic DNA. Translation: CAA74482.1 .
    AL009126 Genomic DNA. Translation: CAB12903.2 .
    Y09476 Genomic DNA. Translation: CAA70668.1 .
    PIRi B39432.
    RefSeqi NP_388944.2. 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 A 1-1232 [» ]
    3U4Q X-ray 2.80 A 1-1232 [» ]
    4CEH X-ray 3.24 A 1-1232 [» ]
    4CEI X-ray 2.80 A 1-1232 [» ]
    4CEJ X-ray 3.00 A 1-1232 [» ]
    ProteinModelPortali P23478.
    SMRi P23478. Positions 11-79.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60825N.
    STRINGi 224308.BSU10630.

    Proteomic databases

    PaxDbi P23478.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12903 ; CAB12903 ; BSU10630 .
    GeneIDi 939793.
    KEGGi bsu:BSU10630.
    PATRICi 18973828. VBIBacSub10457_1108.

    Organism-specific databases

    GenoListi BSU10630. [Micado ]

    Phylogenomic databases

    eggNOGi COG1074.
    HOGENOMi HOG000015621.
    KOi K16898.
    OrthoDBi EOG6HJ22G.
    PhylomeDBi P23478.

    Enzyme and pathway databases

    BioCyci BSUB:BSU10630-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.300. 4 hits.
    3.90.320.10. 1 hit.
    HAMAPi MF_01451. AddA.
    InterProi IPR014152. DNA_helicase_suAddA.
    IPR014017. DNA_helicase_UvrD-like_C.
    IPR000212. DNA_helicase_UvrD/REP.
    IPR011604. Exonuc_phg/RecB_C.
    IPR027417. P-loop_NTPase.
    IPR011335. Restrct_endonuc-II-like.
    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. 3 hits.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsi TIGR02785. addA_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 780.
    5. "Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis."
      Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.
      Microbiology 143:3305-3308(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1000-1232.
      Strain: 168.
    6. "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.
    7. "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, COFACTOR, ATP-DEPENDENCE.
    8. "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.
    9. "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.
    10. "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 LYS-36 AND ASP-1172.
    11. "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: SUBUNIT, DNA-BINDING.

    Entry informationi

    Entry nameiADDA_BACSU
    AccessioniPrimary (citable) accession number: P23478
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 114 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 E.coli 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