UVRB_SYNY3
ID UVRB_SYNY3 Reviewed; 669 AA.
AC Q55170;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=sll0459;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP DISCUSSION OF SOS REGULON.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15225304; DOI=10.1111/j.1365-2958.2004.04100.x;
RA Domain F., Houot L., Chauvat F., Cassier-Chauvat C.;
RT "Function and regulation of the cyanobacterial genes lexA, recA and ruvB:
RT LexA is critical to the survival of cells facing inorganic carbon
RT starvation.";
RL Mol. Microbiol. 53:65-80(2004).
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 -!- MISCELLANEOUS: This bacteria is considerably more resistant to UV and
CC gamma irradiation than E.coli; the E.coli-like SOS regulon model is not
CC an appropriate model for DNA repair in this cyanobacterium.
CC {ECO:0000305|PubMed:15225304}.
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; BA000022; BAA10309.1; -; Genomic_DNA.
DR PIR; S74391; S74391.
DR AlphaFoldDB; Q55170; -.
DR SMR; Q55170; -.
DR IntAct; Q55170; 3.
DR STRING; 1148.1001167; -.
DR PaxDb; Q55170; -.
DR EnsemblBacteria; BAA10309; BAA10309; BAA10309.
DR KEGG; syn:sll0459; -.
DR eggNOG; COG0556; Bacteria.
DR InParanoid; Q55170; -.
DR OMA; EYVDRMV; -.
DR PhylomeDB; Q55170; -.
DR Proteomes; UP000001425; 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.
FT CHAIN 1..669
FT /note="UvrABC system protein B"
FT /id="PRO_0000138438"
FT DOMAIN 27..414
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 431..597
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 628..663
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 93..116
FT /note="Beta-hairpin"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 669 AA; 76849 MW; 9C5B2485AE8A90E3 CRC64;
MTSDLFSLHA PFRPTGDQPT AIASLIESLQ GEHKFQTLLG ATGTGKTFTM ASVIAELGRP
TLVLAHNKTL AAQLCNELRQ FFPENAVEYF ISYYDYYQPE AYIPVTDTYI EKTASINDEI
DMLRHSATRS LFERRDVIVV ASISCIYGLG IPSQYLKAAV PLQVGAEYDP RLVIRDLVNV
QYSRNDVELQ RGRFRLKGDV LEIVPAYEDR VIRIEFFGDE VEALRLIDPV SGEILQSLDR
ISIYPARHFV TPEETLEKAC QQIQTEMEQQ VAFLEKNNLL VEAQRLSQRT RYDLEMLREV
GYCNGVENYS RYLADRQAGE PPECLVDYFP EDWLLVIDES HVTIPQLRGM YNGDQARKKV
LIDHGFRLPS AADNRPLKAE EFWQKVKQCV FVSATPGVWE IEQSEARVIE QVIRPTGVLD
PEIFVRPTTG QVDDLYGEIQ TRVKLKERVL ITTLTKRMAE DLTDYFSERG IKVQYLHSEI
QSIQRIEILQ ALRDGEFDVL IGVNLLREGL DLPEVSLVAI MDADKEGFLR AERSLIQTIG
RAARHIRGQA ILYADNFTDS MQKAIAETER RRKIQQEYNE KHGITPQPIN KRANNAILQF
LDISRRLNSQ QLEEVYEQAQ DLPLEKIPDL IQQLEEKMQE AAKKQEFEVA AIYRDRIQHL
RDRLLGHKK
