UVRB_GLOVI
ID UVRB_GLOVI Reviewed; 680 AA.
AC Q7NJH7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=gll1855;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(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; BA000045; BAC89796.1; -; Genomic_DNA.
DR RefSeq; NP_924801.1; NC_005125.1.
DR RefSeq; WP_011141853.1; NC_005125.1.
DR AlphaFoldDB; Q7NJH7; -.
DR SMR; Q7NJH7; -.
DR STRING; 251221.35212421; -.
DR EnsemblBacteria; BAC89796; BAC89796; BAC89796.
DR KEGG; gvi:gll1855; -.
DR PATRIC; fig|251221.4.peg.1887; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_3; -.
DR InParanoid; Q7NJH7; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR PhylomeDB; Q7NJH7; -.
DR Proteomes; UP000000557; 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; Reference proteome; SOS response.
FT CHAIN 1..680
FT /note="UvrABC system protein B"
FT /id="PRO_0000227317"
FT DOMAIN 27..422
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 443..609
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 93..116
FT /note="Beta-hairpin"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 680 AA; 76909 MW; 93ECE2D09A71DA47 CRC64;
MTDDRFVVSA PYRPTGDQPR AIAQLSAGAL GGVTFQTLLG ATGTGKTFTI ANVIEKVGKP
TLVLAHNKTL AAQLCNELRE FFPDNAVEYF VSYYDYYQPE AYIPQTDTYI EKSASINDEI
DMLRHSATRS LFERRDVIVV ASVSCIYGLG MPEEYLRAAI PLKVGSNIDQ RELLRQLVTV
QYERNDIDLG RGRFRVRGDV VEIGPAYEDR IIRVEFFGDE VEAVRWLDPV TGEVVRSVNS
LNIYPAKHFV TPEEQLEQAC IAIEQELEAR VAELEGENKL LEAQRIKQRT RYDLEMLREV
GYCNGVENYS RHLAARRPGE APSCLIDYFP QDWLLVVDES HVTIPQIRGM YNGDAQRKKV
LIDHGFRLPS AADNRPLKAP EFWDKVRQAI FVSATPGDWE VELSGGGRDP ETGRMAGEHV
AEQIIRPTGV LDPEVFVRPV AGQVDDLLHE IHDRVARRER VLVTTLTKRM AEDLTEYFQE
RGVKVRYLHS EIQAIERIEI LQALRQGDFD VLIGVNLLRE GLDLPEVSLV AILDADKEGF
LRAERSLIQT IGRAARHVRG QVIMYADRLT ASMDKAISET ERRRQIQRAY NAAHGLTPQP
IVKRLDANSI LDYLAVSRRL NQQELEAAAA APAEVALADI PELVSQLEIQ MRDAAKKLEF
EKAAEYRDKI HKLRERLLGK
