ID D2B9S4_STRRD Unreviewed; 711 AA.
AC D2B9S4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=Sros_2983;
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 /
OS NI 9100).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptosporangineae; Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100;
RX DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100T).";
RL Stand. Genomic Sci. 2:29-37(2010).
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 UVR domain.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR EMBL; CP001814; ACZ85937.1; -; Genomic_DNA.
DR RefSeq; YP_003338680.1; NC_013595.1.
DR ProteinModelPortal; D2B9S4; -.
DR EnsemblBacteria; ACZ85937; ACZ85937; Sros_2983.
DR GeneID; 8666270; -.
DR KEGG; sro:Sros_2983; -.
DR PATRIC; 32467943; VBIStrRos112010_2964.
DR HOGENOM; HOG000073580; -.
DR KO; K03702; -.
DR OMA; CIYGLGI; -.
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; 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; 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; Helicase; Hydrolase;
KW Nucleotide-binding; SOS response.
FT DOMAIN 43 227 Helicase ATP-binding (By similarity).
FT DOMAIN 447 613 Helicase C-terminal (By similarity).
FT DOMAIN 666 701 UVR (By similarity).
FT NP_BIND 56 63 ATP (By similarity).
FT MOTIF 109 132 Beta-hairpin (By similarity).
SQ SEQUENCE 711 AA; 80361 MW; 6DD47D52EE4B9E16 CRC64;
MAPPTVGGVR PVTDLQRKVA PFEVVTDMTP SGDQPTAIAE LERRVKAGDK DNVLLGATGT
GKTATVAWLI ERLQRPTLVI QPNKTLAAQF ANELREMMPN NAIEYFVSYY DYYQPEAYVP
QSDTYIEKDS SINDEVERLR HSATNSLLTR RDTIVVASVS CIYGLGTPQE YVDRMTSLKV
GQEIERDSLL RRLVDMQYTR NDLAFTRGTF RVRGDTIEII PKYEELAVRI EMFGDEIEKL
STMHPLTGEV ITEDEELYIF PASHYVAGTE RMEKAVRGIE AELAQTLETM ERQGKLLEAQ
RLRMRTTYDL EMMRQIGTCS GIENYSRHMD GRAPGSAPNT LLDYFPEDFL LVLDESHQTV
PQIGAMYEGD ASRKRTLVEH GFRLPSAMDN RPLKWEEFLE RIDQTVYLSA TPGTYELGRS
KGDVVEQVIR PTGLVDPEVI VKPTKSQIDD LVHEIRTRTE KDERVLVTTL TKKMSEDLTD
YLLELGIRVR YLHSEVDTLR RIELLRELRM GEFDVLVGIN LLREGLDLPE VSLVAILDAD
KEGFLRSETS LIQTIGRAAR NVSGQVHMYA DRITPSMERA IEETNRRRAK QTAYNEANGI
DPQPLRKKIA DILDSLNRED ADTAQLLGGS GRQQSRGKAP VPGFVVKQVG QHAKAIAGEM
PRAQLEALVE SLTDQMHQAA TDLQFEVAAR LRDEIKELKR EVRDMREAGV S
//
