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Database: UniProt
Entry: A0A101V919_9FIRM
LinkDB: A0A101V919_9FIRM
Original site: A0A101V919_9FIRM 
ID   A0A101V919_9FIRM        Unreviewed;       660 AA.
AC   A0A101V919;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=APF76_11575 {ECO:0000313|EMBL:KUO50342.1};
OS   Desulfitibacter sp. BRH_c19.
OC   Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC   Desulfitibacter.
OX   NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO50342.1, ECO:0000313|Proteomes:UP000053015};
RN   [1] {ECO:0000313|EMBL:KUO50342.1, ECO:0000313|Proteomes:UP000053015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO50342.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUO50342.1}.
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DR   EMBL; LOER01000033; KUO50342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101V919; -.
DR   STRING; 1734395.APF76_11575; -.
DR   Proteomes; UP000053015; Unassembled WGS sequence.
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; 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|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587}.
FT   DOMAIN          25..159
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          429..595
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          622..657
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          256..290
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          614..645
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           91..114
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   660 AA;  76048 MW;  7BE612D05602CE42 CRC64;
     MKPFKVVSGY SPKGDQPKAI EQLADGIQGN LKNQILLGAT GTGKTYTMAK VIEKVQKPTL
     VMAHNKILAA QLCSEFRDFF PENSVEYFVS YYDYYQPEAY IPHTDTYIEK DSSLNDEIDK
     MRHSATSALF ERNDVIIVAS VSCIYGLGSP VDYRNLVLSL REGVEYDRDK ILRKLVDIQY
     DRNDYDFHRG TFRVRGDVIE IFPASFTEKA IRVEMFGDEI ERILEIDTFT GEVISQRNHI
     SIFPASHYVI EEDKLKVAIM NIEQELDERL KELKDNNKLV EAQRLEQRTR YDLEMLQEIG
     FCSGIENYSR HLIGKAPGEP PFTLIDYFPE DFLLVIDESH VSVPQIGGMY KGDHSRKQNL
     VEHGFRLPSA LDNRPLKFAE FEKKINQIVF VSATPGPYEL ERTQQTVEQI IRPTGLVDPM
     ISIRPIKGQM DNLYTEIQKR VSKNQRTLVT TLTKRMAEDL TDYFKELGVK VRYMHSDIDT
     IERMEIIRDL RLGEFDVLVG INLLREGLDL PEVSLVVILD ADKEGFLRSD RALIQTMGRA
     ARNIDGQVIM YADKITGSME RAIGETERRR NIQLEFNEKH HITPETVKKE VRKVLEASRV
     AEEKTDYLSK QKINKMAKHE IKDLINQMEK EMKVAASKLE FERAAQLRDI IVDLQKQIGI
//
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