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Protein

ATP-dependent helicase/nuclease subunit A

Gene

addA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi30 – 37ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36K → A: Loss of helicase and nuclease activity. DNA-binding is unaltered. 1 Publication1
Mutagenesisi1172D → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000644491 – 1232ATP-dependent helicase/nuclease subunit AAdd BLAST1232

Proteomic databases

PaxDbiP23478.
PRIDEiP23478.

Interactioni

Subunit structurei

Heterodimer of AddA and AddB.2 Publications

Protein-protein interaction databases

DIPiDIP-60825N.
STRINGi224308.Bsubs1_010100005881.

Structurei

Secondary structure

11232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Helixi13 – 20Combined sources8
Beta strandi26 – 30Combined sources5
Helixi36 – 48Combined sources13
Beta strandi51 – 53Combined sources3
Helixi57 – 59Combined sources3
Beta strandi60 – 63Combined sources4
Helixi67 – 87Combined sources21
Helixi92 – 100Combined sources9
Turni101 – 103Combined sources3
Beta strandi104 – 107Combined sources4
Helixi109 – 120Combined sources12
Helixi121 – 123Combined sources3
Helixi135 – 156Combined sources22
Helixi159 – 168Combined sources10
Helixi175 – 188Combined sources14
Beta strandi191 – 193Combined sources3
Helixi194 – 199Combined sources6
Helixi202 – 205Combined sources4
Turni213 – 215Combined sources3
Helixi219 – 243Combined sources25
Beta strandi246 – 249Combined sources4
Helixi256 – 269Combined sources14
Turni270 – 272Combined sources3
Helixi274 – 283Combined sources10
Beta strandi294 – 297Combined sources4
Helixi299 – 304Combined sources6
Helixi307 – 323Combined sources17
Beta strandi324 – 326Combined sources3
Helixi328 – 362Combined sources35
Helixi368 – 379Combined sources12
Beta strandi380 – 384Combined sources5
Beta strandi387 – 390Combined sources4
Helixi392 – 400Combined sources9
Beta strandi402 – 408Combined sources7
Helixi409 – 411Combined sources3
Helixi414 – 423Combined sources10
Helixi428 – 430Combined sources3
Beta strandi433 – 437Combined sources5
Helixi439 – 441Combined sources3
Turni445 – 448Combined sources4
Helixi452 – 460Combined sources9
Beta strandi461 – 464Combined sources4
Beta strandi466 – 468Combined sources3
Beta strandi470 – 474Combined sources5
Beta strandi476 – 480Combined sources5
Helixi482 – 493Combined sources12
Helixi498 – 501Combined sources4
Turni507 – 509Combined sources3
Beta strandi524 – 530Combined sources7
Helixi546 – 563Combined sources18
Beta strandi568 – 571Combined sources4
Helixi572 – 574Combined sources3
Beta strandi576 – 579Combined sources4
Helixi582 – 584Combined sources3
Beta strandi585 – 594Combined sources10
Helixi595 – 604Combined sources10
Beta strandi605 – 607Combined sources3
Beta strandi609 – 611Combined sources3
Beta strandi614 – 616Combined sources3
Helixi617 – 619Combined sources3
Helixi621 – 634Combined sources14
Helixi639 – 647Combined sources9
Turni649 – 651Combined sources3
Helixi655 – 662Combined sources8
Beta strandi666 – 668Combined sources3
Helixi670 – 680Combined sources11
Helixi686 – 707Combined sources22
Helixi710 – 721Combined sources12
Helixi723 – 727Combined sources5
Helixi733 – 750Combined sources18
Turni752 – 754Combined sources3
Helixi758 – 770Combined sources13
Beta strandi783 – 786Combined sources4
Beta strandi788 – 792Combined sources5
Helixi793 – 795Combined sources3
Turni796 – 798Combined sources3
Beta strandi801 – 807Combined sources7
Helixi816 – 819Combined sources4
Beta strandi820 – 825Combined sources6
Turni826 – 828Combined sources3
Beta strandi829 – 832Combined sources4
Beta strandi834 – 836Combined sources3
Turni837 – 840Combined sources4
Beta strandi841 – 843Combined sources3
Helixi846 – 872Combined sources27
Beta strandi874 – 883Combined sources10
Helixi887 – 897Combined sources11
Beta strandi901 – 904Combined sources4
Turni907 – 911Combined sources5
Helixi917 – 925Combined sources9
Beta strandi926 – 928Combined sources3
Helixi940 – 944Combined sources5
Beta strandi949 – 954Combined sources6
Helixi956 – 959Combined sources4
Helixi973 – 978Combined sources6
Helixi991 – 999Combined sources9
Helixi1005 – 1007Combined sources3
Beta strandi1010 – 1016Combined sources7
Turni1048 – 1050Combined sources3
Helixi1057 – 1068Combined sources12
Helixi1079 – 1091Combined sources13
Helixi1097 – 1102Combined sources6
Helixi1105 – 1109Combined sources5
Helixi1110 – 1113Combined sources4
Helixi1115 – 1121Combined sources7
Beta strandi1124 – 1137Combined sources14
Helixi1138 – 1140Combined sources3
Beta strandi1147 – 1149Combined sources3
Beta strandi1151 – 1163Combined sources13
Beta strandi1168 – 1174Combined sources7
Turni1183 – 1185Combined sources3
Turni1187 – 1189Combined sources3
Helixi1190 – 1196Combined sources7
Helixi1198 – 1212Combined sources15
Beta strandi1216 – 1223Combined sources8
Turni1224 – 1227Combined sources4
Beta strandi1228 – 1231Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 481UvrD-like helicase ATP-bindingAdd BLAST473
Domaini508 – 798UvrD-like helicase C-terminalAdd BLAST291

Sequence similaritiesi

Belongs to the helicase family. AddA subfamily.Curated

Phylogenomic databases

eggNOGiENOG4107R2I. Bacteria.
COG1074. LUCA.
HOGENOMiHOG000015621.
InParanoidiP23478.
KOiK16898.
OMAiENAFEFS.
PhylomeDBiP23478.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
3.90.320.10. 1 hit.
HAMAPiMF_01451. AddA. 1 hit.
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. 4 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti780A → G in AAA22201 (PubMed:1646786).Curated1
Sequence conflicti780A → G in CAA74482 (PubMed:9579061).Curated1

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.
WP_003233100.1. NZ_JNCM01000035.1.

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.
PIRiB39432.
RefSeqiNP_388944.2. NC_000964.3.
WP_003233100.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60825N.
STRINGi224308.Bsubs1_010100005881.

Proteomic databases

PaxDbiP23478.
PRIDEiP23478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107R2I. Bacteria.
COG1074. LUCA.
HOGENOMiHOG000015621.
InParanoidiP23478.
KOiK16898.
OMAiENAFEFS.
PhylomeDBiP23478.

Enzyme and pathway databases

BioCyciBSUB:BSU10630-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
3.90.320.10. 1 hit.
HAMAPiMF_01451. AddA. 1 hit.
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. 4 hits.
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]
ProtoNetiSearch...

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 2, 2016
This is version 128 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.