ID   UVRB_PSEU2              Reviewed;         671 AA.
AC   Q4ZV05;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Psyr_1974;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000075; AAY37017.1; -; Genomic_DNA.
DR   RefSeq; WP_003345654.1; NC_007005.1.
DR   RefSeq; YP_235055.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZV05; -.
DR   SMR; Q4ZV05; -.
DR   STRING; 205918.Psyr_1974; -.
DR   EnsemblBacteria; AAY37017; AAY37017; Psyr_1974.
DR   KEGG; psb:Psyr_1974; -.
DR   PATRIC; fig|205918.7.peg.2016; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_6; -.
DR   OMA; EYVDRMV; -.
DR   Proteomes; UP000000426; 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; SOS response.
FT   CHAIN           1..671
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_0000227351"
FT   DOMAIN          25..412
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          429..582
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          632..667
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   REGION          601..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           91..114
FT                   /note="Beta-hairpin"
FT   COMPBIAS        609..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   671 AA;  76357 MW;  CA72F35F2D24D3FD CRC64;
     MSEFQLVTRF EPAGDQPEAI RQLVEGIDAG LAHQTLLGVT GSGKTFSIAN VISQIKRPTL
     VLAPNKTLAA QLYGEFKAFF PNNAVEYFVS YYDYYQPEAY VPSSDTFIEK DASINDHIEQ
     MRLSATKALL ERKDAIIVTT VSCIYGLGSP ETYLRMVMHI DRGDKLDQRA LLRRLADLQY
     TRNDMDFARA TFRVRGDVID IYPAESDLEA IRVELFDDEV ESLSAFDPLT GEVIRKLPRF
     TFYPKSHYVT PRETLIEAME NIKVELQERL EYLRSQNKLV EAQRLEQRTR FDLEMMLELG
     YCNGIENYSR YLSGRPSGAP PPTLFDYLPP DALLVIDESH VSVPQVGAMY KGDRSRKETL
     VEYGFRLPSA LDNRPMRFDE WEAISPQTIF VSATPGNYEA EHAGRIVEQV VRPTGLVDPQ
     IEIRPALTQV DDLLSEIHKR AALEERVLVT TLTKRMSEDL TDYLSDHGVR VRYLHSDIDT
     VERVEIIRDL RLGTFDVLVG INLLREGLDM PEVSLVAILD ADKEGFLRSD RSLIQTIGRA
     ARNLNGRAIL YADRITGSME RAIGETERRR EKQIAFNLEH GITPKGVFKD VADIMEGATV
     PGSRSKKRKG MAKAAEENAR YENELRSPSE INKRIRQLEE KMYQLARDLE FEAAAQMRDE
     IGKLRERLLA V