ID A0A1F8SDT4_9CHLR Unreviewed; 1319 AA.
AC A0A1F8SDT4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=A2V85_02005 {ECO:0000313|EMBL:OGO58038.1};
OS Chloroflexi bacterium RBG_16_72_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797663 {ECO:0000313|EMBL:OGO58038.1, ECO:0000313|Proteomes:UP000176218};
RN [1] {ECO:0000313|EMBL:OGO58038.1, ECO:0000313|Proteomes:UP000176218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00204}.
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:OGO58038.1}.
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DR EMBL; MGOE01000051; OGO58038.1; -; Genomic_DNA.
DR STRING; 1797663.A2V85_02005; -.
DR Proteomes; UP000176218; 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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
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; cd00081; Hint; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd18790; SF2_C_UvrB; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR HAMAP; MF_00204; UvrB; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
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; TIGR01443; intein_Cterm; 1.
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; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF12344; UvrB; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00204};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW 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|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00204};
KW Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 267..390
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 463..517
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
FT DOMAIN 552..576
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 576..689
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 959..1125
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1156..1191
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 1293..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1145..1179
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 622..645
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 1319 AA; 145975 MW; B6BA06345B0DA6E2 CRC64;
MPDFRLVAPF EPTGDQPQAI ERLVEGLGRG LRHQTLLGAT GTGKSLPGDE PVLIGQEDAD
GRLVWRIRPI GDVVEEALAT RAGGDDRGTC VADGTDGPAA FVVTIDPQTH RPVSARVTAF
TRHASPTELW LVETSDGRRV TVTADHNFVR LASDARLEVV TTAEVRPGDS IPIPTAIPEP
GEPLTRLDTW DAIDAAAAWV AGPEILDDTT AAHARWLLAT GSRAPLGSIG RAGVRTLERY
GPTRVGGRKG KHQLPASRAL DAPYLEFLGL FVAEGHVAGT YATVTPGPAS TRLVTDRLDQ
IGIGWAPRSA GEIVLPARIV ADHLGVLCGH RASDKHLPDF WPQLSNDRLG RLLAGYFEGD
GWVEVNAVCA VTKSEVLANG IAYALLRLGI VGRLSRIWKR AMGTGHQGAW YWQISIRGHD
DIAAFERSAG FLSERKQRRL QEVVTATVGG NIDALPKGAG RHVREARLAL QATQSELADL
LGMSRSAVGL IEGGQRRLRR STGIRLLAAL RHRAAAHRVA EAGLGLGALE RLIACRWATI
HRVTPVPSSG PFVYDFTVAG SETFLAGFGG IIVHNTYVMA QTIVRHQKPT LVLAHNKTLA
AQLYSEFREF FPDNAVEYFV SYFDYYQPEA YLPRSDTYIE KDSSRNEEID RLRHAATHAL
FERRDVIIVA SVSCIYGLGA PVDYGATILR LKVGGQYRRD AVLRHLVDLQ YQRNDAALSR
ARFRVRGDTL EIGPASSEEI VRVEFFGDEV ERITELDPLT GELLAERREL NVYPATHFVT
PREKLGQAIA AIEVEMEERV GQMEAEGRAL EAARLRQRTT FDLEMLRELG YCSGVENYSR
HLSLREPGSR PWTLLDYFPP DWLLIVDESH MTIPQVVGMY KNDRTRKEIL VDFGFRLPSA
LDNRPLTFEE FEVHVNQSLY VSATPGPYEL ERSERVVEQL IRPTGIVDPQ ISVRPTEGQI
DDLLEEIRGR VDRGERALVT TLTKKMAEDL ADYLKELGVK VQYLHSEVDT LERVAILRDL
RLGVYDVLVG INLLREGLDL PEVTLVAILD ADKEGFLRSA WSLIQMIGRA ARNTGGEVVM
YADNVTESMK VAIEETNRRR AVQERYNTEH GIEPQTIIKG IHDINDRLRA VGENRVGYSA
ERRDRDLAEA DKAEVERLVA RMETEMKAAA KQLEFERAAA LRDEIQQIRL RVLEQDQSVV
VARAAERAAK EALLPATERA AAHRPGARAS DAAAAFEVTE VTVLPSGESP AAALDGIPAD
GEDAAGVAAE LFPGIRDEHE DEDGGWQARW LDRPTWDRTV TPNIRRRTGQ RPNRRRRGY
//
