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Protein

UvrABC system protein B

Gene

uvrB

Organism
Bacillus caldotenax
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA2B2 complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage (By similarity).By similarity

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 478ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Excision nuclease

Keywords - Biological processi

DNA damage, DNA excision, DNA repair, SOS response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
UvrABC system protein B
Short name:
Protein UvrB
Alternative name(s):
Excinuclease ABC subunit B
Gene namesi
Name:uvrB
OrganismiBacillus caldotenax
Taxonomic identifieri1395 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillusGeobacillus thermoleovorans group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi98 – 11316QPEAY…YIEKD → G: Inactive in incision, unable to form a stable complex with DNA. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 658657UvrABC system protein BPRO_0000138379Add
BLAST

Interactioni

Subunit structurei

Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.

Structurei

Secondary structure

1
658
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 3013Combined sources
Beta strandi34 – 407Combined sources
Helixi46 – 5712Combined sources
Beta strandi61 – 644Combined sources
Helixi68 – 8114Combined sources
Beta strandi85 – 906Combined sources
Helixi93 – 953Combined sources
Beta strandi96 – 983Combined sources
Beta strandi100 – 1034Combined sources
Turni104 – 1074Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi113 – 1164Combined sources
Helixi119 – 13012Combined sources
Turni131 – 1333Combined sources
Beta strandi137 – 1415Combined sources
Helixi143 – 1464Combined sources
Beta strandi147 – 1493Combined sources
Helixi153 – 1564Combined sources
Beta strandi160 – 1656Combined sources
Turni170 – 1723Combined sources
Helixi173 – 1786Combined sources
Turni179 – 1813Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi192 – 1954Combined sources
Beta strandi197 – 2026Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi220 – 2256Combined sources
Beta strandi226 – 2283Combined sources
Turni229 – 2313Combined sources
Beta strandi239 – 2435Combined sources
Beta strandi246 – 2494Combined sources
Helixi253 – 27624Combined sources
Beta strandi280 – 2834Combined sources
Helixi287 – 29812Combined sources
Beta strandi299 – 3013Combined sources
Helixi306 – 3094Combined sources
Helixi310 – 3134Combined sources
Helixi325 – 3284Combined sources
Beta strandi334 – 3385Combined sources
Helixi340 – 35920Combined sources
Turni360 – 3656Combined sources
Helixi369 – 3735Combined sources
Helixi379 – 3857Combined sources
Beta strandi389 – 3924Combined sources
Helixi398 – 4036Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi421 – 4255Combined sources
Helixi430 – 44314Combined sources
Beta strandi447 – 4515Combined sources
Helixi457 – 46610Combined sources
Turni467 – 4693Combined sources
Beta strandi472 – 4754Combined sources
Turni482 – 4843Combined sources
Helixi485 – 4917Combined sources
Turni492 – 4943Combined sources
Beta strandi497 – 5026Combined sources
Beta strandi506 – 5083Combined sources
Beta strandi514 – 5218Combined sources
Beta strandi522 – 5243Combined sources
Helixi527 – 5293Combined sources
Helixi531 – 5388Combined sources
Helixi539 – 5413Combined sources
Beta strandi548 – 5525Combined sources
Helixi558 – 58023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D9XX-ray2.60A2-658[»]
1D9ZX-ray3.15A2-658[»]
1T5LX-ray2.60A/B2-658[»]
2FDCX-ray3.30A/B2-658[»]
ProteinModelPortaliP56981.
SMRiP56981. Positions 2-651.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56981.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 414388Helicase ATP-bindingAdd
BLAST
Domaini430 – 596167Helicase C-terminalAdd
BLAST
Domaini622 – 65736UVRAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi93 – 11624Beta-hairpinAdd
BLAST

Domaini

The beta-hairpin motif is involved in DNA binding.

Sequence similaritiesi

Belongs to the UvrB family.Curated
Contains 1 helicase ATP-binding domain.Curated
Contains 1 helicase C-terminal domain.Curated
Contains 1 UVR domain.Curated

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
4.10.860.10. 1 hit.
HAMAPiMF_00204. UvrB. 1 hit.
InterProiIPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR001943. UVR_dom.
IPR004807. UvrB.
IPR024759. UvrB_YAD/RRR_dom.
[Graphical view]
PANTHERiPTHR24029. PTHR24029. 1 hit.
PfamiPF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF02151. UVR. 1 hit.
PF12344. UvrB. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF46600. SSF46600. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00631. uvrb. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56981-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEGRFQLVA PYEPQGDQPQ AIAKLVDGLR RGVKHQTLLG ATGTGKTFTI
60 70 80 90 100
SNVIAQVNKP TLVIAHNKTL AGQLYSELKE FFPHNAVEYF VSYYDYYQPE
110 120 130 140 150
AYVPQTDTYI EKDAKINDEI DKLRHSATSA LFERRDVIIV ASVSCIYGLG
160 170 180 190 200
SPEEYRELVV SLRVGMEIER NALLRRLVDI QYDRNDIDFR GTFRVRGDVV
210 220 230 240 250
EIFPASRDEH CIRVEFFGDE IERIREVDAL TGKVLGEREH VAIFPASHFV
260 270 280 290 300
TREEKMRLAI QNIEQELEER LAELRAQGKL LEAQRLEQRT RYDLEMMREM
310 320 330 340 350
GFCSGIENYS RHLALRPPGS TPYTLLDYFP DDFLIIVDES HVTLPQLRGM
360 370 380 390 400
YNGDRARKQV LVDHGFRLPS ALDNRPLTFE EFEQKINQII YVSATPGPYE
410 420 430 440 450
LEHSPGVVEQ IIRPTGLLDP TIDVRPTKGQ IDDLIGEIRE RVERNERTLV
460 470 480 490 500
TTLTKKMAED LTDYLKEAGI KVAYLHSEIK TLERIEIIRD LRLGKYDVLV
510 520 530 540 550
GINLLREGLD IPEVSLVAIL DADKEGFLRS ERSLIQTIGR AARNANGHVI
560 570 580 590 600
MYADTITKSM EIAIQETKRR RAIQEEYNRK HGIVPRTVKK EIRDVIRATY
610 620 630 640 650
AAEETEMYEA KPAAAMTKQE REELIRTLEA EMKEAAKALD FERAAQLRDI

IFELKAEG
Length:658
Mass (Da):75,455
Last modified:January 23, 2007 - v2
Checksum:iEEFCA1C76F56F826
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D9XX-ray2.60A2-658[»]
1D9ZX-ray3.15A2-658[»]
1T5LX-ray2.60A/B2-658[»]
2FDCX-ray3.30A/B2-658[»]
ProteinModelPortaliP56981.
SMRiP56981. Positions 2-651.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56981.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
4.10.860.10. 1 hit.
HAMAPiMF_00204. UvrB. 1 hit.
InterProiIPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR001943. UVR_dom.
IPR004807. UvrB.
IPR024759. UvrB_YAD/RRR_dom.
[Graphical view]
PANTHERiPTHR24029. PTHR24029. 1 hit.
PfamiPF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF02151. UVR. 1 hit.
PF12344. UvrB. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF46600. SSF46600. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00631. uvrb. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUVRB_BACCA
AccessioniPrimary (citable) accession number: P56981
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 100 of the entry and version 2 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

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.