ID UVRB_AROAE Reviewed; 685 AA.
AC Q5P0E7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 29-MAY-2013, entry version 67.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=AZOSEA30920; ORFNames=ebA5438;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. A damage recognition complex composed
CC of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC binding by UvrB and probably causes local melting of the DNA
CC helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC strands. Then UvrB probes one DNA strand for the presence of a
CC lesion. If a lesion is found the UvrA subunits dissociate and the
CC UvrB-DNA preincision complex is formed. This complex is
CC subsequently bound by UvrC and the second UvrB is released. If no
CC lesion is found, the DNA wraps around the other UvrB subunit that
CC will check the other stand for damage (By similarity).
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the UvrB family.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 1 UVR domain.
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DR EMBL; CR555306; CAI09217.1; -; Genomic_DNA.
DR RefSeq; YP_160118.1; NC_006513.1.
DR ProteinModelPortal; Q5P0E7; -.
DR SMR; Q5P0E7; 18-608.
DR STRING; 76114.ebA5438; -.
DR EnsemblBacteria; CAI09217; CAI09217; ebA5438.
DR GeneID; 3182843; -.
DR KEGG; eba:ebA5438; -.
DR PATRIC; 20972398; VBIAroAro98752_3125.
DR eggNOG; COG0556; -.
DR HOGENOM; HOG000073580; -.
DR KO; K03702; -.
DR OMA; CIYGLGI; -.
DR ProtClustDB; PRK05298; -.
DR BioCyc; AARO76114:GJTA-3135-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:HAMAP.
DR GO; GO:0004386; F:helicase activity; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:HAMAP.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR Gene3D; 4.10.860.10; -; 1.
DR HAMAP; MF_00204; UvrB; 1; -.
DR InterPro; IPR006935; Helicase/UvrB_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR004807; UvrB.
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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF46600; UvrB_C; 1.
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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW DNA repair; Excision nuclease; Nucleotide-binding; SOS response.
FT CHAIN 1 685 UvrABC system protein B.
FT /FTId=PRO_0000227278.
FT DOMAIN 39 420 Helicase ATP-binding.
FT DOMAIN 443 596 Helicase C-terminal.
FT DOMAIN 640 675 UVR.
FT NP_BIND 52 59 ATP (Potential).
FT MOTIF 105 128 Beta-hairpin.
SQ SEQUENCE 685 AA; 77530 MW; 32F8A07BDD261925 CRC64;
MTSSTDSVPV ITFADSPFRL HQPFPPAGDQ PAAIELLTEG IGDGLMYQTL LGVTGSGKTY
TMANVIARCG RPALVLAPNK TLAAQLYAEF REFFPENAVE YFVSYYDYYQ PEAYVPSRDL
FIEKDSSINE HIEQMRLSAT KSLMERRDVV IVATVSCIYG IGDPVDYHAM ILHLREGERI
AHRDLVQRLV AMQYTRSDID FRRGTFRVRG DVIDVFPAEN AELAVRIEMF DDEVEHLTLF
DPLTGHLKQK LVRFTVYPSS HYVTPRATVL KAIEAIKDEL RDRSAWFQTS GKLVEAQRIE
QRTRFDLEML NEMGFCKGIE NYSRHLSGRG QGEPPPTLID YLPSDALLFV DESHVSIPQV
GGMYKGDRSR KENLVGYGFR LPSALDNRPL KFEEFERLMP QTIFVSATPS TYEAEHQGQV
VEQVVRPTGL IDPAIDVRPA TTQVDDLLSE AKRRIAVGER VLVTTLTKRM AEDLTDYLAE
NGIRVRYLHS DIDTVERVEI IRDLRLGKFD VLVGINLLRE GLDIPEVSLV AILDADKEGF
LRSERSLIQT IGRAARHING RAILYADVVT RSMRAAIDET ERRRVKQIAF NQANGIVPKT
VSKRIKDIID GVYGGDVERD GRSVAEPPPE YFSMNEKTVA KSIRKLEKEM QEHARNLEFE
KAAAARDELF RLRQRTFGAD QHGTP
//
