ID C7RAN9_KANKD Unreviewed; 662 AA.
AC C7RAN9;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Kkor_0911 {ECO:0000313|EMBL:ACV26331.1};
OS Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV26331.1, ECO:0000313|Proteomes:UP000001231};
RN [1] {ECO:0000313|EMBL:ACV26331.1, ECO:0000313|Proteomes:UP000001231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC {ECO:0000313|Proteomes:UP000001231};
RX PubMed=21304661; DOI=10.4056/sigs.36635;
RA Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL Stand. Genomic Sci. 1:226-233(2009).
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; CP001707; ACV26331.1; -; Genomic_DNA.
DR RefSeq; WP_012800845.1; NC_013166.1.
DR AlphaFoldDB; C7RAN9; -.
DR STRING; 523791.Kkor_0911; -.
DR KEGG; kko:Kkor_0911; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_6; -.
DR InParanoid; C7RAN9; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000001231; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000001231};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00204}.
FT DOMAIN 26..159
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 430..592
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 623..658
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 257..284
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 619..658
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 92..115
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 662 AA; 75285 MW; 3B0AE710AB3F2A50 CRC64;
MSQQFDIHSP FPPAGDQPKA IKQLLEGLED GLSHQTLLGV TGSGKTYTMA NVIAQSGRPA
IIMAPNKTLA AQLYGEMKEF FPNNAVEYFV SYYDYYQPEA YVAASDTFIE KDSSINEHIE
QMRLSATRAL LERRDTIIVA SVSAIYGLGD PKAFHSMVMH LKVGDEVDQR FILRRLAELQ
YTRNEFDLQR ATYRVRGDLI DIYPAESEKH AIRIELFDDE VETIQTFDPL TGEVLKRLTR
VTVFPKSHYV TSRQTILDAI EQIKVDLKER LAQFYEQNKL VEAQRLEQRV KFDIEMMQEL
GYCSGIENYS RYLSGAQPGE PPPCLLDYLP PDALMLIDES HVTVSQIGAM YKGDRSRKET
LVNYGFRLPA ALDNRPLKFE EFERITPQTV FVSATPGKYE EENTGQIVEQ VVRPTGLIDP
EVEIRPVGTQ VDDLLSEIHL RVEKNERVLV TTLTKRMAED LTDYLSEHGA RVRYLHSDID
TVERMEIIRD LRLGEFDVLV GINLLREGLD MPEVSLVAIL DADKEGFLRS ERSLIQTIGR
AARNLSGKAI LYADRITGSM ERAIGETNRR RAIQQEYNEK HGITPIGVSK KITDVMDTGH
SKKSRKVAEK LSQYKVKSLA DAVKEIAHME KQMLEHAKNL EFEKAAKMRD EIQKLREASL
AS
//
