UVRB_GEMAT
ID UVRB_GEMAT Reviewed; 700 AA.
AC C1A4H0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=GAU_1953;
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC Gemmatimonas.
OX NCBI_TaxID=379066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505;
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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; AP009153; BAH38995.1; -; Genomic_DNA.
DR RefSeq; WP_012683442.1; NC_012489.1.
DR AlphaFoldDB; C1A4H0; -.
DR SMR; C1A4H0; -.
DR STRING; 379066.GAU_1953; -.
DR EnsemblBacteria; BAH38995; BAH38995; GAU_1953.
DR KEGG; gau:GAU_1953; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_0; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000002209; 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..700
FT /note="UvrABC system protein B"
FT /id="PRO_1000204134"
FT DOMAIN 26..183
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 631..666
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT REGION 608..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 700 AA; 78628 MW; 3B9628FDB29CFBB5 CRC64;
MTAPFRLHAP FAPAGDQPRA ITELSSGLHR GDRIQTLLGV TGSGKTMTMA NVIADWGRPT
LVLSHNKTLA AQLYGELKSF FPNNAVEYFI SYYDYYQPEA YVPSSDTYIE KDASINEDID
RLRLRATSSL MERDDVVIVS TVSAIYGLGD PVQYRERMVA LSRGQQIARD DILRALVGIQ
YLRNDVAFER GTFRVRGDTV EILPAYEEQA VRIELWGDEI ERISKIDPVT GETIAALERM
AIYPAKHFIT NRPTIERASM AIRDELATRL AELRMAGKLL EAQRLEQRTQ FDLEMLMEIG
TCAGIENYSR HISGREAGER PACLLDYFPD DYLVVVDESH VTLPQIRAMY NGDRARKLTL
VDYGFRLPSA LDNRPLVFDE FMSLVPRLVN VSATPGELEL QLSEGVVVEQ VIRPTGLLDP
VLEVRPVKGQ VDDLLHEIRA RERRGERVLV TTLTKRMSED LTDYLQQMGV RVRYMHSDID
AIERMEIVRG LRLGEFDVLV GINLLREGLD MPEVSLVAIL DADQEGFLRS DRSLIQTIGR
AARNLHGMAI LYGDRITGSM QRAIDETTRR RTIQREHNEA HGIVPRGVTK SVDEVRFITR
VADARVEREG EAPAPRRLAS ESAPRSREEL ETLVGELEIA MREAAVALDF EAAARLRDQL
FEVRTALGQA PSEARGNAQA PKRPPGSAPQ RRAGGGRRGR
