UVRB_TROW8
ID UVRB_TROW8 Reviewed; 677 AA.
AC Q83NI7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=TW477;
OS Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=218496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW08/27;
RX PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA Relman D.A.;
RT "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT Tropheryma whipplei.";
RL Lancet 361:637-644(2003).
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}.
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DR EMBL; BX251411; CAD67144.1; -; Genomic_DNA.
DR RefSeq; WP_011096424.1; NC_004551.1.
DR AlphaFoldDB; Q83NI7; -.
DR SMR; Q83NI7; -.
DR GeneID; 67388253; -.
DR KEGG; tws:TW477; -.
DR HOGENOM; CLU_009621_2_1_11; -.
DR OMA; EYVDRMV; -.
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..677
FT /note="UvrABC system protein B"
FT /id="PRO_0000227380"
FT DOMAIN 31..417
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 434..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 629..664
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 97..120
FT /note="Beta-hairpin"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 677 AA; 77101 MW; 1B7554D875554283 CRC64;
MYKNLHPKYF RLAAEYDPSG DQPKAIGELS DRIESGETDI VLLGATGTGK SATIAWLIEK
LARPTLIIAH NKTLAAQLAN EFRKFFPDNA VEYFVSYYDY YQPEAYVPKT DTFIEKDASV
NSEVERLRHR ATTSLLTRRD VIVVATVSCI YGLGAPSEYL KAGFRLEVGQ KISQRVLLER
FTQLQYNRND VGFERGNFRV RGDTIEIIPV YEEYTVRIEM WGDEIERVLC LHPVTGNLLS
EQRGVLIFPA SHYVTSSENL KRAIVDIRKE LQQRLRYFKR NNSLLEAQRL ETRTEYDIEL
MEQLGFCSGI ENYSRHIDGR APGEPPFCLL DYFDDDFLTV IDESHVTVPQ IGSMHAGDFS
RKKALVENGF RLPSAIDNRP LCFDEFRQRV GQVIYLSATP GKYELSKSDG VVEQIIRPTG
LVDPKITVKP IKGQIDDLLE EIRKRKLLSE RVLVTTLTKR MAEELTDFLS EAGVNVSYLH
SDIDTLHRVE LLTSLRMGRI DVLVGINLLR EGLDLPEVSL VAILDADKEG FLRSTTSFIQ
TIGRAARHVS GEVHMYADNM TESMQKSIDE TNRRRRIQQD YNRKMGVTPV PIKKTVSDIT
EVLSRPSRKI DCTILDSLPD PKIDGKQIKS HIKSLEAKMY MAAESLMFEE AAELRDEIQS
LKEKFLKPRG SGGKIRQ
