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UVRB_NEIGO
ID   UVRB_NEIGO              Reviewed;         675 AA.
AC   Q50939;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=7721686; DOI=10.1128/jb.177.8.1952-1958.1995;
RA   Black C.G., Fyfe J.A.M., Davies J.K.;
RT   "A promoter associated with the neisserial repeat can be used to transcribe
RT   the uvrB gene from Neisseria gonorrhoeae.";
RL   J. Bacteriol. 177:1952-1958(1995).
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; U11547; AAA75358.1; -; Genomic_DNA.
DR   PIR; B56262; B56262.
DR   RefSeq; WP_003688978.1; NZ_UGRM01000002.1.
DR   AlphaFoldDB; Q50939; -.
DR   SMR; Q50939; -.
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; SOS response.
FT   CHAIN           1..675
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_0000138414"
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"
SQ   SEQUENCE   675 AA;  76989 MW;  7F1756AA3E0A9CF5 CRC64;
     MEVIRYPNSP FKLHQPFPPA GDQPTAIAGL LEGLSDGLAY QTLLGVTGSG KTYTMANVIA
     QSGRPAIIMA HNKTLAAQLY AEMREFFPEN AVEYFVSYYD YYQPEAYVPS RDLFIEKDSA
     INEHIEQMRL SATKNLMTRD DVIIVATVSA IYGIGDPTEY QQMVLSVKEG DTIEQRDIIA
     TLVSMQYERG DLDFKRGSFR VRGDVIDVYP AESSENALRI SLFDDEIDRL DMFDPLSGSL
     HQRVGRYTVF PSSHYVTPRD TVLRACESIK EELRERIEFF AREQRPVEQQ RIEQRTRFDL
     EMLYEMGFCK GIENYSRHFS GKKEGEPPPT LMDYLPDNAI MFIDESHVTV TQIGGMYKGD
     ASRKQNLVDY GFRLPSARDN RPLKFHEFEK VMPQTVFVSA TPAKYEEEHA GQVVEQVVRP
     TGLVDPQIII RPVATQVDDL MSEINDRIQK GERVLVTTLT KRMAEQLTDY YSELGIKVRY
     LHSDIDTVER VEIIRDLRLG LFDVLVGINL LREGLDIPEV SLVAILDADK EGFLRSHRSL
     IQTIGRAARN VNGVAILYAD KITDSMKAAV DETERRREKQ IKFNEEHGIV PQQIKKQVKD
     IIDGVYHEED SGKGRRQGKN KVKVGEIHNE EDAIKEIAKL EKAMQQAARD LQFEEAAVLR
     DRIRNIKENL LFGAE
 
 
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