ID   A1IGB7_PHOPO            Unreviewed;       675 AA.
AC   A1IGB7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00009141};
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   ECO:0000313|EMBL:BAF43690.1};
OS   Photobacterium phosphoreum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=659 {ECO:0000313|EMBL:BAF43690.1};
RN   [1] {ECO:0000313|EMBL:BAF43690.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 13896 {ECO:0000313|EMBL:BAF43690.1};
RA   Kasai S.;
RT   "Identification of luxO in Photobacterium phosphoreum IFO 13896.";
RL   Submitted (JAN-2003) 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, ECO:0000256|SAAS:SAAS00009130}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
CC       ECO:0000256|SAAS:SAAS00088351}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01200955}.
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|HAMAP-
CC       Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
CC       ECO:0000256|SAAS:SAAS00538712}.
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DR   EMBL; AB101000; BAF43690.1; -; Genomic_DNA.
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:ATPase 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   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 {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01200956}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|SAAS:SAAS01200952};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
KW   ECO:0000256|SAAS:SAAS01200947};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00240303};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
KW   ECO:0000256|SAAS:SAAS01200950};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00009139};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01200961};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00088434}.
FT   DOMAIN          26..159
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          432..598
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          635..670
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   NP_BIND         39..46
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   COILED          265..285
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           92..115
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   675 AA;  76639 MW;  4F58FAA7DD96A344 CRC64;
     MSKLFNLVSD YSPAGDQPTA IEQLMDGLDS GLAQQTLLGV TGSGKTFTIA NVIAQANRPT
     LIMAPNKTLA AQLYGEMRDF FPDNAVEYFV SYYDYYQPEA YVPTTDTFIE KDASVNAHIE
     QMRLSATKAL MERRDVIIIA SVSAIYGLGD PESYLKMMLH VRRGDVLDQR DILRRLAELQ
     YKRNDAVFER GTFRVRGEVI DIFPAESEKE AIRLELFDGE VEVISSFDPL TGAIIQRNLA
     RTTIYPKTHY VTPREKILDA IEGIKLELTQ RKQQLLDNNK LVEEQRISQR TQFDIEMMNE
     LGFCSGIENY SRYLSGRTEG EPPPTLFDYL PADGLLIIDE SHVTVSQIGA MFRGDRSRKE
     NLVEYGFRLP SALDNRPMKF EEFESLAPQT IYVSATPGNY EIEKSGGDIA EQVVRPTGLL
     DPEIEVRPVA TQVDDLLSEI HIRSAKQERV LVTTLTKRMS EDLTEYLTEH GVKVRYLHSD
     IDTVERVEII RDLRLGKFDV LVGINLLREG LDIPEVSLVA ILDADKEGFL RSERSLIQTM
     GRAARNIEGK AILYGDRITG SMERAINETQ RRREKQIIYN LEHNIIPQKL NKKIGDLLEL
     GAPSGRSKSR NKAADLHKVA ESKGTYSVLT PQQLELEIQR LEKQMYDFAQ NLEFEQAADT
     RDKIHQLRQQ FIANS
//