ID A0A367FTF3_9ACTN Unreviewed; 703 AA.
AC A0A367FTF3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=DQ384_01075 {ECO:0000313|EMBL:RCG33072.1};
OS Sphaerisporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sphaerisporangium.
OX NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG33072.1, ECO:0000313|Proteomes:UP000253094};
RN [1] {ECO:0000313|EMBL:RCG33072.1, ECO:0000313|Proteomes:UP000253094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG33072.1,
RC ECO:0000313|Proteomes:UP000253094};
RA Li L.;
RT "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT the South China Sea.";
RL Submitted (JUN-2018) 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:RCG33072.1}.
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DR EMBL; QOIL01000001; RCG33072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367FTF3; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000253094; 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}; Reference proteome {ECO:0000313|Proteomes:UP000253094};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 35..158
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 439..592
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 658..693
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 654..700
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 101..124
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 703 AA; 79478 MW; 2BEF557074CB8C53 CRC64;
MRPVTDLQRR VAPFEVVTDM SPSGDQPTAI AELERRVKGG EKDNVLLGAT GTGKTATVAW
LIERLQRPAL VMQPNKTLAA QFANELREML PNNAVEYFVS YYDYYQPEAY VPQTDTYIEK
DSSINDEVDR LRHSATNSLL TRRDTVVVAS VSCIYGLGTP QEYVDRMVRL KVGQEVERDR
LLRRLVDMQY ARNDLSFTRG TFRVRGDTIE VIPQYEELAV RIEMFGDEIE KLSTLHPLTG
EVITEDQELY IFPASHYVAG PERMERAIGD IEAELATTLA TMEKQGKLLE AQRLRMRTTY
DIEMMRQVGT CSGIENYSRH IDGRGPGTAP NTLLDYFPED FLLVLDESHQ TVPQIGAMYE
GDASRKRTLV DHGFRLPSAM DNRPLKWEEF LDRIGQTVYL SATPGPYELG RSKGDVVEQV
IRPTGLVDPE VIVKQTKGQI DDLVHEIRER ADRDERVLVT TLTKKMAEDL TDYLLELGIR
VRYLHSEVDT LRRIELLREL RMGEYDVLVG INLLREGLDL PEVSLVAILD ADKEGFLRSE
TSLIQTIGRA ARNVSGQVHM YADRVTPSME RAIDETNRRR AKQVAYNKAN GIDPKPLRKK
IADILDSLAR EDADTDRLLG AGRQQSRGKA PVPGMAAARQ AGQHAKTIAG EMPRAQLESL
VQSLTEQMHT AAADLQFEVA ARLRDEIKEL KRELRDMREA GVH
//
