UVRB_CHLL2
ID UVRB_CHLL2 Reviewed; 684 AA.
AC B3EFX1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Clim_0411;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001097; ACD89504.1; -; Genomic_DNA.
DR RefSeq; WP_012465385.1; NC_010803.1.
DR AlphaFoldDB; B3EFX1; -.
DR SMR; B3EFX1; -.
DR STRING; 290315.Clim_0411; -.
DR PRIDE; B3EFX1; -.
DR EnsemblBacteria; ACD89504; ACD89504; Clim_0411.
DR KEGG; cli:Clim_0411; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_10; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000008841; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; SOS response.
FT CHAIN 1..684
FT /note="UvrABC system protein B"
FT /id="PRO_1000099540"
FT DOMAIN 30..188
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 435..601
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 641..676
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 96..119
FT /note="Beta-hairpin"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 684 AA; 77927 MW; EA0714B5A2B756E3 CRC64;
MYGITGNGYR LVSSYSPKGD QPKAIEQLVE GVQRGDRWQT LLGVTGSGKT FTISNLIAQV
GKPVLVMSHN KTLAAQLYGE LRQFFPDNAV EYFISYYDFY QPEAYLPALD KYIAKDLRIN
DEIERLRLKA TSSLLSGRRD VIVVSSVSCI YGLGSPEEWK AQIIELRPGM EKDRDQFLQE
LVSLHYVRDD MKPGPGKFRV RGDIIDLVPA HEELAVRVEF FGPEIESLQT FDMQSGEVLG
RDDYAFIYPA RQFVAGEEQM RHAMLAIENE LAGRLNELRG ENRLIEARRL EERTRYDLEM
MKELGYCSGI ENYSRHLAGR EPGDRPHCLL DYFPEDYLVV VDESHVTLPQ IRGMYGGDRS
RKTILVEHGF RLPSALDNRP LRFDEYVGLV PQVVCVSATP GDLELEYSGG VIVEQLVRPT
GLLDPPVEVR PVKGQIDDLL GEIRKHTARG FKALIMTLTK RMSEDLDDYF RKTGIRSRYL
HSEIKSLERM QILRELRTGE IDVLVGVNLL REGLDLPEVS LVAILDADKE GFLRNTRSLM
QIAGRAARNS EGFVVLYADV LTRSIREVLD ETSRRRKIQQ AYNEEHGIVP QSIIKSVEQV
LNTTGVADAE ERYRRKRFGL EPKPERLLST LIDTLTAEEC YSMAESLRLE MQEAALKMEY
EKAAYLRDEI TKFEHRANEA GKGI
