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P23478

- ADDA_BACSU

UniProt

P23478 - ADDA_BACSU

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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

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

Mg2+1 PublicationNote: 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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP23478.
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

        10         20         30         40         50
MNIPKPADST WTDDQWNAIV STGQDILVAA AAGSGKTAVL VERMIRKITA
60 70 80 90 100
EENPIDVDRL LVVTFTNASA AEMKHRIAEA LEKELVQRPG SLHIRRQLSL
110 120 130 140 150
LNRASISTLH SFCLQVLKKY YYLIDLDPGF RIADQTEGEL IGDEVLDELF
160 170 180 190 200
EDEYAKGEKA FFELVDRYTT DRHDLDLQFL VKQVYEYSRS HPNPEAWLES
210 220 230 240 250
FVHLYDVSEK SAIEELPFYQ YVKEDIAMVL NGAKEKLLRA LELTKAPGGP
260 270 280 290 300
APRADNFLDD LAQIDELIQH QDDFSELYKR VPAVSFKRAK AVKGDEFDPA
310 320 330 340 350
LLDEATDLRN GAKKLLEKLK TDYFTRSPEQ HLKSLAEMKP VIETLVQLVI
360 370 380 390 400
SYGKRFEAAK QEKSIIDFSD LEHYCLAILT AENDKGEREP SEAARFYQEQ
410 420 430 440 450
FHEVLVDEYQ DTNLVQESIL QLVTSGPEET GNLFMVGDVK QSIYRFRLAE
460 470 480 490 500
PLLFLSKYKR FTESGEGTGR KIDLNKNFRS RADILDSTNF LFKQLMGGKI
510 520 530 540 550
GEVDYDEQAE LKLGAAYPDN DETETELLLI DNAEDTDASE EAEELETVQF
560 570 580 590 600
EAKAIAKEIR KLISSPFKVY DGKKKTHRNI QYRDIVILLR SMPWAPQIME
610 620 630 640 650
ELRAQGIPVY ANLTSGYFEA VEVAVALSVL KVIDNPYQDI PLASVLRSPI
660 670 680 690 700
VGADENELSL IRLENKKAPY YEAMKDYLAA GDRSDELYQK LNTFYGHLQK
710 720 730 740 750
WRAFSKNHSV SELIWEVYRD TKYMDYVGGM PGGKQRQANL RVLYDRARQY
760 770 780 790 800
ESTAFRGLFR FLRFIERMQE RGDDLGTARA LSEQEDVVRL MTIHSSKGLE
810 820 830 840 850
FPVVFVAGLG RNFNMMDLNK SYLLDKELGF GTKYIHPQLR ISYPTLPLIA
860 870 880 890 900
MKKKMRRELL SEELRVLYVA LTRAKEKLFL IGSCKDHQKQ LAKWQASASQ
910 920 930 940 950
TDWLLPEFDR YQARTYLDFI GPALARHRDL GDLAGVPAHA DISGHPARFA
960 970 980 990 1000
VQMIHSYDLL DDDLEERMEE KSERLEAIRR GEPVPGSFAF DEKAREQLSW
1010 1020 1030 1040 1050
TYPHQEVTQI RTKQSVSEIK RKREYEDEYS GRAPVKPADG SILYRRPAFM
1060 1070 1080 1090 1100
MKKGLTAAEK GTAMHTVMQH IPLSHVPSIE EAEQTVHRLY EKELLTEEQK
1110 1120 1130 1140 1150
DAIDIEEIVQ FFHTEIGGQL IGAKWKDREI PFSLALPAKE IYPDAHEADE
1160 1170 1180 1190 1200
PLLVQGIIDC LYETEDGLYL LDYKSDRIEG KFQHGFEGAA PILKKRYETQ
1210 1220 1230
IQLYTKAVEQ IAKTKVKGCA LYFFDGGHIL TL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P23478.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 116 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