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Database: UniProt
Entry: B1XTQ7_POLNS
LinkDB: B1XTQ7_POLNS
Original site: B1XTQ7_POLNS 
ID   B1XTQ7_POLNS            Unreviewed;       718 AA.
AC   B1XTQ7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|ARBA:ARBA00029504, ECO:0000256|HAMAP-Rule:MF_00204};
DE            Short=Protein UvrB {ECO:0000256|HAMAP-Rule:MF_00204};
DE   AltName: Full=Excinuclease ABC subunit B {ECO:0000256|HAMAP-Rule:MF_00204};
GN   Name=uvrB {ECO:0000256|HAMAP-Rule:MF_00204};
GN   OrderedLocusNames=Pnec_0467 {ECO:0000313|EMBL:ACB43734.1};
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB43734.1};
RN   [1] {ECO:0000313|EMBL:ACB43734.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1 {ECO:0000313|EMBL:ACB43734.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.;
RT   "Complete sequence of Polynucleobacter necessarius STIR1.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00026033, ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
CC   -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000256|ARBA:ARBA00008533,
CC       ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
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DR   EMBL; CP001010; ACB43734.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1XTQ7; -.
DR   STRING; 452638.Pnec_0467; -.
DR   KEGG; pne:Pnec_0467; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_4; -.
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   CDD; cd17916; DEXHc_UvrB; 1.
DR   CDD; cd18790; SF2_C_UvrB; 1.
DR   Gene3D; 6.10.140.240; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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   NCBIfam; TIGR00631; uvrb; 1.
DR   PANTHER; PTHR24029; UVRABC SYSTEM PROTEIN B; 1.
DR   PANTHER; PTHR24029:SF0; UVRABC SYSTEM PROTEIN B; 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; C-terminal UvrC-binding domain of UvrB; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00204}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00204};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00204}.
FT   DOMAIN          71..205
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          475..641
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          672..707
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          668..695
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           137..160
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   COMPBIAS        15..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         84..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   718 AA;  81339 MW;  C3749A3BED94D6D8 CRC64;
     MIAEMPSKLP KIGPNSEVKV DKKSPAADPL GEAGHDLDPA KFITFPDSLY QLYQPFAPAG
     DQPQAIDALV EGIEDGLTFQ TLLGVTGSGK TFTMANVIAR TGRPAIIFAP NKTLAAQLYS
     EFREFFPKNA VEYFVSYYDY YQPEAYVPQR DLFIEKDSSI NEHIEQMRLS ATKSLLERRD
     VVIVATVSAI YGIGNPGDYH SMVMTLRPGD KMSQRDILMR LIAMQYDRNE TDFKRGVFRV
     RGDTIDIFPA EHNELAVRVE LFDDVIESLQ FFDPLTGKIR QKIPQFTVYP SSHYVTPRDT
     VLKAIETIKT ELRTRLDEFV KDGKLVEAQR LEQRTRFDLE MLNELGFCKG IENYSRHLSG
     AAPGEAPPTL VDYLPNDAVM FLDESHVLIG QLNAMYNGDK SRKHTLVEFG FRLPSAMDNR
     PLKFAEFETK MRQTIFVSAT PADYEGTHQG QVVEQVARPT GLVDPEIEVL PASTQVDDLL
     DQIHARVKVG ERVLVTVLTK RMAEQLTDYL SDNGVKVRYV HSDIDTVERV EILRDLRLGV
     FDVLVGINLL REGLDIPEVS LVAILDADKE GFLRSERSLI QTIGRAARNV RGKAILYADR
     ITDSMKRAMG ETERRRTKQI AFNKLHGIEP KGVQKRIKDI IDGVYDVKEK RQEMQIEQER
     ARYEDMGEKD LVAEIKRLEK QMNAEAKNLE FEKAAGTRDR LTKVKEMAFG ARSRDSIG
//
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