UVRB_THET8
ID UVRB_THET8 Reviewed; 665 AA.
AC Q56243; Q5SH38;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=TTHA1892;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-12, AND ATPASE
RP ACTIVITY.
RX PubMed=8621636; DOI=10.1074/jbc.271.16.9612;
RA Kato R., Yamamoto N., Kito K., Kuramitsu S.;
RT "ATPase activity of UvrB protein form Thermus thermophilus HB8 and its
RT interaction with DNA.";
RL J. Biol. Chem. 271:9612-9618(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10578047; DOI=10.1093/oxfordjournals.jbchem.a022566;
RA Nakagawa N., Sugahara M., Masui R., Kato R., Fukuyama K., Kuramitsu S.;
RT "Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme
RT of nucleotide excision repair.";
RL J. Biochem. 126:986-990(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
RX PubMed=10518516; DOI=10.1073/pnas.96.21.11717;
RA Machius M., Henry L., Palnitkar M., Deisenhofer J.;
RT "Crystal structure of the DNA nucleotide excision repair enzyme UvrB from
RT Thermus thermophilus.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11717-11722(1999).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The ATPase activity is stimulated by single-stranded
CC DNA. UvrB is stable up to 80 Celsius degrees.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000305}.
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DR EMBL; D49912; BAA08653.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71715.1; -; Genomic_DNA.
DR RefSeq; WP_011228991.1; NC_006461.1.
DR RefSeq; YP_145158.1; NC_006461.1.
DR PDB; 1C4O; X-ray; 1.50 A; A=2-665.
DR PDB; 1D2M; X-ray; 1.90 A; A=1-665.
DR PDB; 7EGT; X-ray; 2.58 A; A/C=1-408.
DR PDBsum; 1C4O; -.
DR PDBsum; 1D2M; -.
DR PDBsum; 7EGT; -.
DR AlphaFoldDB; Q56243; -.
DR SMR; Q56243; -.
DR STRING; 300852.55773274; -.
DR EnsemblBacteria; BAD71715; BAD71715; BAD71715.
DR GeneID; 3168014; -.
DR KEGG; ttj:TTHA1892; -.
DR PATRIC; fig|300852.9.peg.1859; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_0; -.
DR OMA; EYVDRMV; -.
DR PhylomeDB; Q56243; -.
DR EvolutionaryTrace; Q56243; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA excision; DNA repair; Excision nuclease;
KW Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..665
FT /note="UvrABC system protein B"
FT /id="PRO_0000138440"
FT DOMAIN 23..408
FT /note="Helicase ATP-binding"
FT DOMAIN 425..591
FT /note="Helicase C-terminal"
FT DOMAIN 611..646
FT /note="UVR"
FT MOTIF 89..112
FT /note="Beta-hairpin"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 478
FT /note="E -> K (in Ref. 1; BAA08653)"
FT /evidence="ECO:0000305"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1D2M"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:1D2M"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1D2M"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1D2M"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:1D2M"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1D2M"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1D2M"
FT HELIX 251..271
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 275..295
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 335..358
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 393..398
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 450..462
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:1C4O"
FT TURN 515..518
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 526..533
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:1C4O"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:1C4O"
FT HELIX 553..576
FT /evidence="ECO:0007829|PDB:1C4O"
SQ SEQUENCE 665 AA; 76160 MW; 68502BFCB6F28BEF CRC64;
MTFRYRGPSP KGDQPKAIAG LVEALRDGER FVTLLGATGT GKTVTMAKVI EALGRPALVL
APNKILAAQL AAEFRELFPE NAVEYFISYY DYYQPEAYVP GKDLYIEKDA SINPEIERLR
HSTTRSLLTR RDVIVVASVS AIYGLGDPRE YRARNLVVER GKPYPREVLL ERLLELGYQR
NDIDLSPGRF RAKGEVLEIF PAYETEPIRV ELFGDEVERI SQVHPVTGER LRELPGFVLF
PATHYLSPEG LEEILKEIEK ELWERVRYFE ERGEVLYAQR LKERTLYDLE MLRVMGTCPG
VENYARYFTG KAPGEPPYTL LDYFPEDFLV FLDESHVTVP QLQGMYRGDY ARKKTLVDYG
FRLPSALDNR PLRFEEFLER VSQVVFVSAT PGPFELAHSG RVVEQIIRPT GLLDPLVRVK
PTENQILDLM EGIRERAARG ERTLVTVLTV RMAEELTSFL VEHGIRARYL HHELDAFERQ
ALIRDLRLGH YDCLVGINLL REGLDIPEVS LVAILDADKE GFLRSERSLI QTIGRAARNA
RGEVWLYADR VSEAMQRAIE ETNRRRALQE AYNLEHGITP ETVRKEVRAV IRPEGYEEAP
LEADLSGEDL RERIAELELA MWQAAEALDF ERAARLRDEI RALEARLQGV RAPEPVPGGR
KRKRR
