ID A0A0F7PH85_9EURY Unreviewed; 689 AA.
AC A0A0F7PH85;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=HLASA_2191 {ECO:0000313|EMBL:ALG83060.1}, HLASF_2157
GN {ECO:0000313|EMBL:AKH98618.1};
OS Halanaeroarchaeum sulfurireducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halanaeroarchaeum.
OX NCBI_TaxID=1604004 {ECO:0000313|EMBL:AKH98618.1, ECO:0000313|Proteomes:UP000069906};
RN [1] {ECO:0000313|EMBL:AKH98618.1, ECO:0000313|Proteomes:UP000069906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR2 {ECO:0000313|EMBL:AKH98618.1,
RC ECO:0000313|Proteomes:UP000069906};
RX PubMed=25978546;
RA Sorokin D.Y., Kublanov I.V., Gavrilov S.N., Rojo D., Roman P.,
RA Golyshin P.N., Slepak V.Z., Smedile F., Ferrer M., Messina E., La Cono V.,
RA Yakimov M.M.;
RT "Elemental sulfur and acetate can support life of a novel strictly
RT anaerobic haloarchaeon.";
RL ISME J. 0:0-0(2015).
RN [2] {ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|Proteomes:UP000060390};
RA Messina E., Kublanov I.V., Toshchakov S., Arcadi E., La Spada G.,
RA La Cono V., Yakimov M.M.;
RT "Complete genome sequence of Halanaeroarchaeum sulfurireducens type strain
RT M27-SA2, a sulfate-reducer haloarchaeon from marine anoxic lake Medee.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALG83060.1, ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|EMBL:ALG83060.1,
RC ECO:0000313|Proteomes:UP000060390};
RX PubMed=27182430; DOI=10.1186/s40793-016-0155-9;
RA Messina E., Sorokin D.Y., Kublanov I.V., Toshchakov S., Lopatina A.,
RA Arcadi E., Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Complete genome sequence of 'Halanaeroarchaeum sulfurireducens' M27-SA2, a
RT sulfur-reducing and acetate-oxidizing haloarchaeon from the deep-sea
RT hypersaline anoxic lake Medee.";
RL Stand. Genomic Sci. 11:35-35(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}.
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DR EMBL; CP008874; AKH98618.1; -; Genomic_DNA.
DR EMBL; CP011564; ALG83060.1; -; Genomic_DNA.
DR RefSeq; WP_050049263.1; NZ_CP011564.1.
DR AlphaFoldDB; A0A0F7PH85; -.
DR STRING; 1604004.HLASA_2191; -.
DR GeneID; 26011521; -.
DR KEGG; hsf:HLASA_2191; -.
DR KEGG; hsu:HLASF_2157; -.
DR PATRIC; fig|1604004.4.peg.2257; -.
DR HOGENOM; CLU_009621_2_1_2; -.
DR OrthoDB; 8371at2157; -.
DR Proteomes; UP000060390; Chromosome.
DR Proteomes; UP000069906; 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; 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:UP000069906};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 40..173
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 443..605
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 632..667
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 628..655
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 106..129
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 689 AA; 77716 MW; A9A82A76C188D5B1 CRC64;
MSDETGPLAP DQPGAEGPFE VDAPFDPAGD QAQAIEELVR GYEQGMEKQT LLGVTGSGKT
NTVSWVVEEL QQPTLVIAHN KTLAAQLYEE FRNLFPDNAV EYFVSYYDYY QPEAYVEQSD
TYIDKDASIN EEIDRLRHSA TRSLLTRDDV IIVASVSAIY GLGDPSNYED MALRLEVGQE
IDRDDLLGGL VDLNYERNDV DFTQGTFRVR GDTVEVFPMY GRYAVRVEFW GEEIERLTKL
DPLEGSVVSE EPAVLVHPAE HYSMPESTLE QAIEEIEADL DERVGYFERT GDLVAAQRIE
ERTTFDLEML REAGYCSGIE NYSVYLSDRE VGEAPYTLLD YFPDDFLTVI DESHRTVPQI
KGQHAGDRSR KESLVENGFR LPTAFDNRPL TFEEFEQKTD RTLYVSATPS DYEREVSDQV
VEQIVRPTYL VDPAVEVEPA ADQIDDLMDR IDRRAENDER VLVTTLTKRM AEDLTEYLEE
AGVAVEYMHD ETDTLERHEL VRGLRLGEFD VLVGINLLRE GLDIPEVSLV AILDADQEGF
LRSRTSLIQT MGRAARNVEG TVVLYADETT DAMEEAIEET QRRRRIQRAF NEEHGTDPTT
IEKAVGEIDL PGSKTDTSSI TGEGPADADE ASVLIEDLED RMQEAADNLE FELAADIRDR
IRKLREEFDL DSGDGVAPDD GLAPEADRF
//
