UVRB_BACCA
ID UVRB_BACCA Reviewed; 658 AA.
AC P56981;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB;
OS Bacillus caldotenax.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1395;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=10601012; DOI=10.1093/emboj/18.24.6899;
RA Theis K., Chen P.J., Skorvaga M., Van Houten B., Kisker C.;
RT "Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision
RT repair.";
RL EMBO J. 18:6899-6907(1999).
RN [2]
RP IMPORTANCE OF THE BETA-HAIRPIN MOTIF, AND MUTAGENESIS OF 98-GLN--ASP-113.
RX PubMed=11687584; DOI=10.1074/jbc.m108847200;
RA Skorvaga M., Theis K., Mandavilli B.S., Kisker C., Van Houten B.;
RT "The beta-hairpin motif of UvrB is essential for DNA binding, damage
RT processing, and UvrC-mediated incisions.";
RL J. Biol. Chem. 277:1553-1559(2002).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. A damage recognition complex composed of 2
CC UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of
CC the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps
CC around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB
CC and probably causes local melting of the DNA helix, facilitating
CC insertion of UvrB beta-hairpin between the DNA strands. Then UvrB
CC probes one DNA strand for the presence of a lesion. If a lesion is
CC found the UvrA subunits dissociate and the UvrB-DNA preincision complex
CC is formed. This complex is subsequently bound by UvrC and the second
CC UvrB is released. If no lesion is found, the DNA wraps around the other
CC UvrB subunit that will check the other stand for damage (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000305}.
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DR PDB; 1D9X; X-ray; 2.60 A; A=2-658.
DR PDB; 1D9Z; X-ray; 3.15 A; A=2-658.
DR PDB; 1T5L; X-ray; 2.60 A; A/B=2-658.
DR PDB; 2FDC; X-ray; 3.30 A; A/B=2-658.
DR PDB; 6O8E; X-ray; 2.61 A; A/B=2-593.
DR PDB; 6O8F; X-ray; 2.81 A; A/B=2-593.
DR PDB; 6O8G; X-ray; 2.64 A; A/B/C=2-593.
DR PDB; 6O8H; X-ray; 2.39 A; A=2-593.
DR PDBsum; 1D9X; -.
DR PDBsum; 1D9Z; -.
DR PDBsum; 1T5L; -.
DR PDBsum; 2FDC; -.
DR PDBsum; 6O8E; -.
DR PDBsum; 6O8F; -.
DR PDBsum; 6O8G; -.
DR PDBsum; 6O8H; -.
DR AlphaFoldDB; P56981; -.
DR SMR; P56981; -.
DR EvolutionaryTrace; P56981; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_00204; UvrB; 1.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR004807; UvrB.
DR InterPro; IPR041471; UvrB_inter.
DR InterPro; IPR024759; UvrB_YAD/RRR_dom.
DR PANTHER; PTHR24029; PTHR24029; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF12344; UvrB; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46600; SSF46600; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00631; uvrb; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50151; UVR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Nucleotide-binding; SOS response.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..658
FT /note="UvrABC system protein B"
FT /id="PRO_0000138379"
FT DOMAIN 27..414
FT /note="Helicase ATP-binding"
FT DOMAIN 430..596
FT /note="Helicase C-terminal"
FT DOMAIN 622..657
FT /note="UVR"
FT MOTIF 93..116
FT /note="Beta-hairpin"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 98..113
FT /note="QPEAYVPQTDTYIEKD->G: Inactive in incision, unable to
FT form a stable complex with DNA."
FT /evidence="ECO:0000269|PubMed:11687584"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1D9X"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1D9X"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1T5L"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:1D9X"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1T5L"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2FDC"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1D9X"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1T5L"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 208..228
FT /evidence="ECO:0007829|PDB:6O8H"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1D9X"
FT HELIX 253..276
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 280..299
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 340..363
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 430..443
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 481..493
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 497..506
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:6O8H"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:1D9X"
FT HELIX 531..538
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:6O8H"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:6O8G"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:6O8H"
FT HELIX 558..581
FT /evidence="ECO:0007829|PDB:6O8H"
SQ SEQUENCE 658 AA; 75455 MW; EEFCA1C76F56F826 CRC64;
MVEGRFQLVA PYEPQGDQPQ AIAKLVDGLR RGVKHQTLLG ATGTGKTFTI SNVIAQVNKP
TLVIAHNKTL AGQLYSELKE FFPHNAVEYF VSYYDYYQPE AYVPQTDTYI EKDAKINDEI
DKLRHSATSA LFERRDVIIV ASVSCIYGLG SPEEYRELVV SLRVGMEIER NALLRRLVDI
QYDRNDIDFR GTFRVRGDVV EIFPASRDEH CIRVEFFGDE IERIREVDAL TGKVLGEREH
VAIFPASHFV TREEKMRLAI QNIEQELEER LAELRAQGKL LEAQRLEQRT RYDLEMMREM
GFCSGIENYS RHLALRPPGS TPYTLLDYFP DDFLIIVDES HVTLPQLRGM YNGDRARKQV
LVDHGFRLPS ALDNRPLTFE EFEQKINQII YVSATPGPYE LEHSPGVVEQ IIRPTGLLDP
TIDVRPTKGQ IDDLIGEIRE RVERNERTLV TTLTKKMAED LTDYLKEAGI KVAYLHSEIK
TLERIEIIRD LRLGKYDVLV GINLLREGLD IPEVSLVAIL DADKEGFLRS ERSLIQTIGR
AARNANGHVI MYADTITKSM EIAIQETKRR RAIQEEYNRK HGIVPRTVKK EIRDVIRATY
AAEETEMYEA KPAAAMTKQE REELIRTLEA EMKEAAKALD FERAAQLRDI IFELKAEG
