ID A0A1A9NPY1_9PROT Unreviewed; 688 AA.
AC A0A1A9NPY1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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=A7976_07770 {ECO:0000313|EMBL:OAJ72055.1};
OS Methylobacillus sp. MM3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=1848039 {ECO:0000313|EMBL:OAJ72055.1, ECO:0000313|Proteomes:UP000077549};
RN [1] {ECO:0000313|EMBL:OAJ72055.1, ECO:0000313|Proteomes:UP000077549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM2 {ECO:0000313|EMBL:OAJ72055.1,
RC ECO:0000313|Proteomes:UP000077549};
RA Macey M.C., Murrell J.C.;
RT "Draft genome of Methylobacillus sp. MM2 isolated from grassland soil.";
RL Submitted (MAY-2016) 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:OAJ72055.1}.
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DR EMBL; LXTQ01000001; OAJ72055.1; -; Genomic_DNA.
DR RefSeq; WP_067107156.1; NZ_LXTQ01000001.1.
DR AlphaFoldDB; A0A1A9NPY1; -.
DR STRING; 1848039.A7976_07770; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000077549; 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; 6.10.140.240; -; 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:UP000077549};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00204}.
FT DOMAIN 42..175
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 446..612
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 643..678
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 639..678
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 108..131
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 688 AA; 78637 MW; 326B48DA62836717 CRC64;
MSNLTNSTPP PEIVTYPGSR YELHQLFPPA GDQPAAIERL TEGLRQGMKY QTLLGVTGSG
KTYTMANVIA RLGRPAIVMA PNKTLAAQLY SEFREFFPNN AVEYFVSYYD YYQPEAYVPS
RDLFIEKDSS INDHIEQMRL SATKSLLERE DSIIVATVSA IYGIGDPGEY HGMVLHIHNG
MKISQRDVIM HLTRMQYDRN EFDFARGTFR VRGDVLDVFP SENSETAVRI SLFDDEIESI
TLFDPLTGQI YNKIHNFRIF PSSHYVTARE ATLRAMETIR QELRERVDFF IKTNKLVEAQ
RIEQRTRYDL EMLNEIGFCK GIENYSRHLT GRGVGEPPPT LIDYLPKNAL MIIDESHVTV
PQIGGMYKGD RARKENLVDY GFRLPSALDN RPLRFEEFEK VMRQCVFVSA TPADYEATHQ
EQVVEQVARP TGLIDPEIIV KPADTQVDDL LSEIKLRVTD RERVLVTTLT KRMAEDLTDY
LAEHGIKVRY LHSDIDTVER VEIIRDLRLG EFDVLVGINL LREGLDIPEV SLVAVLDADK
EGFLRSERSL IQTSGRAARN LNGKVIFYAN RITRSMKLAM DETERRRKKQ MAFNEANGIT
PRGVVKRIKD IIDGVYDAEA GKKELQAAQT FANYHAMNEK QVVKELKRLE KEMHDAAKNL
EFEKAAKLRD ELKNLRAQFY GAEPPDAT
//
