UVRB_BACHK
ID UVRB_BACHK Reviewed; 658 AA.
AC Q6HBC2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204};
DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204};
DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204};
GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; OrderedLocusNames=BT9727_4845;
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP-
CC Rule:MF_00204}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017355; AAT63851.1; -; Genomic_DNA.
DR RefSeq; WP_000441046.1; NC_005957.1.
DR RefSeq; YP_039154.1; NC_005957.1.
DR AlphaFoldDB; Q6HBC2; -.
DR SMR; Q6HBC2; -.
DR EnsemblBacteria; AAT63851; AAT63851; BT9727_4845.
DR GeneID; 64200810; -.
DR KEGG; btk:BT9727_4845; -.
DR PATRIC; fig|281309.8.peg.5151; -.
DR HOGENOM; CLU_009621_2_1_9; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000001301; Chromosome.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Nucleotide-binding; SOS response.
FT CHAIN 1..658
FT /note="UvrABC system protein B"
FT /id="PRO_0000227285"
FT DOMAIN 26..413
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 430..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 622..657
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 92..115
FT /note="Beta-hairpin"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 658 AA; 75164 MW; 830AE6A9D3550021 CRC64;
MERQFEIVSA YSPQGDQPVA IEKLVEGINS GKKKQVLLGA TGTGKTFTIS NVIKEVQKPT
LVMAHNKTLA GQLYSELKDF FPNNAVEYFV SYYDYYQPEA YVPQTDTFIE KDAQINDEID
KLRHSATSAL FERDDVIIVA SVSCIYGLGS PEEYRELVVS LRVGMEKDRN QLLRELVDVQ
YGRNDIDFKR GTFRVRGDVV EIFPASLDEH CIRIEFFGDE IDRIREVNAL TGEVLAERDH
VAIFPASHFV TREEKMKVAI ENIEKELEER LKELNDNGKL LEAQRIEQRT RYDLEMMREM
GFCSGIENYS RHLTLRPAGA TPYTLLDYFP EDFLIVMDES HVSVPQVRAM YNGDQARKQV
LVDHGFRLPS ALDNRPLTFD EFEEKTNQVI YVSATPGPYE LEQSPEVIEQ IIRPTGLLDP
PIDIRPIEGQ IDDLLGEIQD RIAKNERVLI TTLTKKMSED LTDYLKDVGI KVNYLHSEVK
TLERIEIIRD LRLGKFDVLV GINLLREGLD IPEVSLVAIL DADKEGFLRS ERSLIQTIGR
AARNENGRVI MYADRITRSM GIAIEETKRR RSIQEAYNEE HGITPKTIQK GVRDVIRATT
AAEEPETYEA TPAKKMTKKE REKTIAKMEA EMKEAAKALD FERAAELRDL LLELKAEG
