UVRB_NEIMB
ID UVRB_NEIMB Reviewed; 675 AA.
AC O33395;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 128.
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=NMB1331;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SD / Serogroup B / Serotype 15 / Subtype 16;
RA Kizil G., Wilks K.E., Palmer H.M., Ala'Aldeen D.A.A.;
RT "Detection and characterisation of meningococcal ultraviolet resistance
RT gene (uvrB).";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; Y14299; CAA74675.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF41706.1; -; Genomic_DNA.
DR PIR; F81095; F81095.
DR RefSeq; NP_274350.1; NC_003112.2.
DR RefSeq; WP_002244151.1; NC_003112.2.
DR AlphaFoldDB; O33395; -.
DR SMR; O33395; -.
DR STRING; 122586.NMB1331; -.
DR PaxDb; O33395; -.
DR EnsemblBacteria; AAF41706; AAF41706; NMB1331.
DR KEGG; nme:NMB1331; -.
DR PATRIC; fig|122586.8.peg.1669; -.
DR HOGENOM; CLU_009621_2_1_4; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000000425; 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..675
FT /note="UvrABC system protein B"
FT /id="PRO_0000138416"
FT DOMAIN 32..417
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 436..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 634..669
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 98..121
FT /note="Beta-hairpin"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT CONFLICT 449
FT /note="E -> Q (in Ref. 1; CAA74675)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="Q -> H (in Ref. 1; CAA74675)"
FT /evidence="ECO:0000305"
FT CONFLICT 611..612
FT /note="GS -> SG (in Ref. 1; CAA74675)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..617
FT /note="LK -> RQ (in Ref. 1; CAA74675)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="D -> N (in Ref. 1; CAA74675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 76914 MW; 6F2634F34EB77D43 CRC64;
MEVIQYPNSP FKLHQPFPPA GDQPTAIAGL LEGLSDGLAY QTLLGVTGSG KTYTMANVIA
QSGRPAIIMA HNKTLAAQLY AEMREFFPEN AVEYFVSYYD YYQPEAYVPS RDLFIEKDSA
INEHIEQMRL SATKNLMTRN DVIIVATVSA IYGIGDPTEY QQMVLSVKEG DTIEQRDIIA
TLVSMQYERG DLDFKRGSFR VRGDVIDVYP AESSENALRI SLFDDEIDRL DMFDPLSGSL
IQRVGRYTVF PSSHYVTPRD TVLRACESIK EELRERIEFF AREQRPVEQQ RIEQRTRFDL
EMLYEMGFCK GIENYSRHFS GKKEGEPPPT LMDYLPDNAI MFIDESHVTV TQIGGMYKGD
ASRKQNLVDY GFRLPSARDN RPLKFHEFEK VMPQTIFVSA TPAKYEEEHA GQVVEQVVRP
TGLVDPQIII RPVATQVDDL MSEINDRIEK GERVLVTTLT KRMAEQLTDY YSELGIKVRY
LHSDIDTVER VEIIRDLRLG LFDVLVGINL LREGLDIPEV SLVAILDADK EGFLRSHRSL
IQTIGRAARN VNGVAILYAD KITDSMKAAI DETERRREKQ IKFNEEQGIV PQQIKKQVKD
IIDGVYHEED GSKGRLKGKN KVKVGEIHNE EDAIKEIAKL EKAMQQAARD LQFEEAAVLR
DRIRDIKENL LFGAE
