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UVRB_COXBU
ID   UVRB_COXBU              Reviewed;         672 AA.
AC   Q83E18;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=CBU_0518;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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; AE016828; AAO90064.1; -; Genomic_DNA.
DR   RefSeq; NP_819550.1; NC_002971.3.
DR   RefSeq; WP_010957630.1; NZ_CCYB01000051.1.
DR   AlphaFoldDB; Q83E18; -.
DR   SMR; Q83E18; -.
DR   STRING; 227377.CBU_0518; -.
DR   EnsemblBacteria; AAO90064; AAO90064; CBU_0518.
DR   GeneID; 1208403; -.
DR   KEGG; cbu:CBU_0518; -.
DR   PATRIC; fig|227377.7.peg.512; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_6; -.
DR   OMA; TEYHQMI; -.
DR   Proteomes; UP000002671; 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..672
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_0000227306"
FT   DOMAIN          26..413
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          430..592
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   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   672 AA;  77336 MW;  CDD1EA5814C4C9F9 CRC64;
     MSKAFKLTSK FKPSGDQPQA IEKLVAGLED GLAYQTLLGV TGSGKTFTIA NAIEKVQRPT
     LILEPNKTLA AQFYAEMREF FPENAVEYFV SYYDYYQPEA YVPSSDTYIE KDASINDHIE
     QMRLSATKAI TERHDTIIIA TVSAIYGLGD PDSYLKMLLH LTRGDQIDQR KILQRLAELQ
     YTRNDLELRR ATYRVNGDII DIYPADSERE AVRVELFDDE VENLSYFDPL TGEMLRRVPR
     ITVYPKTHYV TPREKLLSTL DQIKIELKER LSQLEKANKL VERQRLEQRT KFDMEMILEL
     GYCSGIENYS RYLSGRNEGE PPPTLIDYLP KDALLIIDES HVTIPQLGGM YRGDRARKET
     LVEYGFRLPS ALDNRPLRFD EFEKLAPQTI FISATPGPYE EKQSDQVVEL LVRPTGLIDP
     EIEVRPVATQ VDDLLSEIKK RAAQNERVLV TTLTKRMAED LTEYFTEHNV RVRYLHSDID
     TVERVEIIRD LRLGVFDVLV GINLLREGLD IPEVSLVAIL DADKEGFLRS ERSLIQTMGR
     AARNVHGKAI LYADRITDSM KRAMEEAERR RIAQSAYNEK HHITPKSIQK AVTEIIEGAR
     TYTERGRFVN QAQLIAEEEA KYIAMTPKQL AKELRKLEEQ MYHHARNLEF EEAAAVRDKI
     QHIRKGLLEV KE
 
 
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