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Database: UniProt
Entry: A8F0V9
LinkDB: A8F0V9
Original site: A8F0V9 
ID   UVRB_RICM5              Reviewed;         661 AA.
AC   A8F0V9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   31-JUL-2019, entry version 75.
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};
GN   OrderedLocusNames=RMA_0273;
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5;
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria:
RT   evidence from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(2007).
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. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000683; ABV84545.1; -; Genomic_DNA.
DR   RefSeq; WP_012152522.1; NC_009900.1.
DR   SMR; A8F0V9; -.
DR   PRIDE; A8F0V9; -.
DR   EnsemblBacteria; ABV84545; ABV84545; RMA_0273.
DR   KEGG; rms:RMA_0273; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   Proteomes; UP000001311; 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: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   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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Helicase; Hydrolase;
KW   Nucleotide-binding; SOS response.
FT   CHAIN         1    661       UvrABC system protein B.
FT                                /FTId=PRO_1000077916.
FT   DOMAIN       25    182       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      430    592       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      621    656       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      38     45       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        91    114       Beta-hairpin.
SQ   SEQUENCE   661 AA;  75351 MW;  19D16A1CD648854B CRC64;
     MNNFSIISEY KPAGDQPKAI DEIIAGLSSK KRSQILLGIT GSGKTFTMAN IIERTNRPTL
     IMAHNKTLAA QIYSEMKSIF PKNAVEYFVS YYDYYQPEAY IARTDTFIEK DSSINEQIDL
     MRHAATRSLL ERRDVIVVSS VSCIYGLGSP DLYYQMMVNL EPGQSYPRDQ LLNDLINLQY
     ERNDIGFERG CFRVKGDNID IFPSHYSNKA WRLSFFGNEL EYIHEFDPLT GAKLAKLDKA
     MVFGNSHFVM PQETVNNAIS GIEEELQKRL EFLKSQDKPL ETQRLNQRTQ YDLEMLTETG
     NCKGVENYSR FFTGRNAGEP PPTLFEYLPE DALLFVDESH VSVPQIRAMY NGDRARKEVL
     VEHGFRLPSA LDNRPLKFEE WEKFRPQTVF VSATPGPFEL EETGGTVVEL IIRPTGLLDP
     ECIIKPATNQ IEDLISEIQT TIAKGFRVLV TTLTKKMAED LTAYLQELKY KTSYLHSHVH
     TLERIEILRD LRQGTIDILV GINLLREGLD IPECGLVAIL DADKEGFLRS EVSLIQTIGR
     AARNSEGRVI LYADKMTKSI DKAVSETLRR RQIQQEYNAK HGIIPKTINR TIHALAEFEK
     IDSKLDKKQA HTLFDNPAKL KTHIDKLKKE MLKAASNLEF EQAAKLRDQL KTLEEAALEL
     S
//
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