ID A0A0G1J5H9_9BACT Unreviewed; 683 AA.
AC A0A0G1J5H9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=UvrABC system protein B {ECO:0000256|ARBA:ARBA00029504, ECO:0000256|RuleBase:RU003587};
GN ORFNames=UW26_C0004G0009 {ECO:0000313|EMBL:KKT39322.1};
OS Candidatus Collierbacteria bacterium GW2011_GWF1_44_12.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618402 {ECO:0000313|EMBL:KKT39322.1, ECO:0000313|Proteomes:UP000034097};
RN [1] {ECO:0000313|EMBL:KKT39322.1, ECO:0000313|Proteomes:UP000034097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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|RuleBase:RU003587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU003587}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000256|ARBA:ARBA00008533,
CC 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:KKT39322.1}.
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DR EMBL; LCHQ01000004; KKT39322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1J5H9; -.
DR PATRIC; fig|1618402.3.peg.175; -.
DR Proteomes; UP000034097; 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-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
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 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};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003587};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769,
KW ECO:0000256|RuleBase:RU003587};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU003587};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881,
KW ECO:0000256|RuleBase:RU003587};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW SOS response {ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 24..204
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 445..612
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 650..683
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 683 AA; 77958 MW; 16EE81765F07388A CRC64;
MDFKIKADFV PTGDQPLAIR KLSDSIKKQN PHQTLLGVTG SGKTFTIAKI IEETQLPTLI
VCHNKTLASQ LYQEFRDFFP DNAVSYFVSY YDYYQPEAYI PQTDTYIEKE ADINPEIDKL
RLTTTANLLS RPDSIVIASV SCIYNIGSPA NQEEFILPLT KGQVISRETI IRRLTDLQYQ
RTSAELTRGF FRAIGQTVQL FPSYMDKVIS FVFDGSVLKD INVLDPYNFT KIEHDDLEHT
GRITINPAKL FITNPQNQQA SLTQIKSDLA VRVAELKLAG KIIEAHRLEQ KVNYDLSMME
EVGYVNGIEN YSRYFDGRKP GEAPYSLLEY FNYNAKKFGK SGFLTVVDES HISLPQIRGM
YNGDQARKEN LINFGFRLES ARDNRPLTYS EFQSRTPIKL YSSATPGEHE LGLSQTAPIP
TVAEQLIRPT GLLDPEVFVH ETKGQIDDLT KEIIKRKERG ERSLVLTMTK RMAEDLTDHF
KDKYGLKVEY LHSDIKTLDR ADILDSLRTG DFDCLVGINL LREGLDLPEV SLVAILDADK
EGFLRTSTAL IQTMGRAARH SSGQVILYAD RISDSMKKAM EETARRRETQ IKYNLDHGIT
PQTIIKPIRE RLLKRDDQLG QVPRIKELAE HGWTEIEDID PETLTPQKKK SLVVKLKKMM
TRAANDWNFE LASRYRDTIK KLQ
//
