ID D0WGD0_SLAES Unreviewed; 719 AA.
AC D0WGD0;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
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 ECO:0000313|EMBL:EEZ61543.1};
GN ORFNames=HMPREF0762_00881 {ECO:0000313|EMBL:EEZ61543.1};
OS Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 /
OS KCTC 5966 / S-7).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=649764 {ECO:0000313|EMBL:EEZ61543.1, ECO:0000313|Proteomes:UP000006001};
RN [1] {ECO:0000313|EMBL:EEZ61543.1, ECO:0000313|Proteomes:UP000006001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 /
RC S-7 {ECO:0000313|Proteomes:UP000006001};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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:EEZ61543.1}.
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DR EMBL; ACUX02000006; EEZ61543.1; -; Genomic_DNA.
DR RefSeq; WP_006362136.1; NZ_GG700630.1.
DR AlphaFoldDB; D0WGD0; -.
DR STRING; 649764.HMPREF0762_00881; -.
DR GeneID; 85007451; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_11; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000006001; 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}; Hydrolase {ECO:0000313|EMBL:EEZ61543.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00204}; Reference proteome {ECO:0000313|Proteomes:UP000006001};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 48..200
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 451..617
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 647..682
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 285..312
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 650..689
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 114..137
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 719 AA; 81197 MW; A819067EBB9D94FB CRC64;
MSSHLKNIEG AVMEGKLPEV RLSSEPFKVV SPYEPSGDQP QAIASLAEGV ERGLRYQTLL
GVTGSGKTFT MAKTIEAVQK PTLVMAPNKT LAAQLAAELK EFFPHNAVVY FVSYYDYYQP
EAYVPQTDTF IEKDASINEE VEKLRHAATS SLLSRRDVIV VASVSCIYGI GSPMDYAGMA
VFVDRQKPAE RDDVIHQLID IQYDRNDYEL SRGTFRVRGD ALDVFPPYAD NPLRIEFWGD
EIESIQEIDN LTGEVLMSFE AIPIWPASHY VTARPKMRKA IGTIQEELRG RLEQLRAEGK
LLEAQRLEMR TNYDLEMLET MGFCSGIENY SRHLDGRSPG EPPYTLIDYF PDDFLCIIDE
SHVTVPQIRG MHEGDRSRKV TLAEHGFRLP SCLDNRPLRF DEFEERVPQF IYVSATPGDY
ENRVSERRVE QIIRPTGLLD PEIEVRPIAS QIDDIIDEAR ARSDAHERVL ITTLTKKMAE
DLTDHLLDQG IRSRYMHSDI GTLERVEILR DLRTGEFDVL VGINLLREGL DLPEVTLVAI
LDADKEGFLR NHRSLIQTIG RAARNVSGKV IMYADKITDS MDLAITETRR RRAIQMAYNE
EHGIEPKTIR KAINDVMGFI TDGDNNEVGT AEDVNKVLAE LSRGEVMRII AGMEEEMASA
SESMDFEEAA RLRDQVVKLR AQMEGTDERD VLADLKKTAR KGSAFGNRKN AAYGSSRRS
//
