ID A0A0B0DFV0_9MICC Unreviewed; 715 AA.
AC A0A0B0DFV0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=AS25_04440 {ECO:0000313|EMBL:KHE75022.1};
OS Kocuria marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=223184 {ECO:0000313|EMBL:KHE75022.1, ECO:0000313|Proteomes:UP000030664};
RN [1] {ECO:0000313|EMBL:KHE75022.1, ECO:0000313|Proteomes:UP000030664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO9-6 {ECO:0000313|EMBL:KHE75022.1,
RC ECO:0000313|Proteomes:UP000030664};
RA Castro D.B., Pereira L.B., Silva M.V., Silva B.P., Zanardi B.R., Carlos C.,
RA Belgini D.R., Limache E.G., Lacerda G.V., Nery M.B., Gomes M.B., Souza S.,
RA Silva T.M., Rodrigues V.D., Paulino L.C., Vicentini R., Ferraz L.F.,
RA Ottoboni L.M.;
RT "High-quality draft genome sequence of Kocuria marina SO9-6, an
RT actinobacterium isolated from a copper mine.";
RL Submitted (SEP-2014) 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:KHE75022.1}.
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DR EMBL; JROM01000016; KHE75022.1; -; Genomic_DNA.
DR RefSeq; WP_035962083.1; NZ_JROM01000016.1.
DR AlphaFoldDB; A0A0B0DFV0; -.
DR STRING; 223184.AS25_04440; -.
DR eggNOG; COG0556; Bacteria.
DR Proteomes; UP000030664; 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};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 35..192
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 438..604
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 670..705
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 624..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 666..712
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 715 AA; 80691 MW; 7737F2DAA459F029 CRC64;
MSLAQKINRV VAPFEVVSEY QPAGDQPKAI ADLSRRIKGG EKDVVLMGAT GTGKSATAAW
LIEAVQRPTL LLVQNKTLAA QLANELRELL PHNAVEYFVS YYDYYQPEAY VPQTDTFIEK
DSSINEEVER LRHSATNALL TRRDTVVVST VSCIYGLGTP EEYVKQMVTL AVGQEMDRDT
LLRQFVNMQY VRNDVDFHRG TFRVRGDTVE IIPMYEELAV RIEFFGDEIE AIYTLHPLTG
EIVNEEQEMY VFPASHYVAG AERMASAIES IQKELQERLQ ELESQNKLVE AQRLRMRTTY
DLEMMEQMGY CNGIENYSLH IDGRPRGSAP HCLLDYFPDD FLLIIDESHV TVPQIGGMYE
GDMSRKRTLV EHGFRLPSAM DNRPLKWDEF LERIGQTMYM SATPGPYEMS KVDSVVEQII
RPTGLVDPQV IVKPTKGQID DLLEQIELRV ERDERVLVTT LTKRMAEDLT EYLMEHGVRV
QYLHSDVDTL KRVELLRDLR MGTFDVLVGI NLLREGLDLP EVSLVAILDA DKEGFLRSTT
SLIQTIGRAA RNVSGEVHMY ADKITNSMNV AIEETNRRRE IQVAYNEEHG IDPQPLRKRI
ADITDQLARE DEDTRTLLAQ RAAANNHTAP VKGGKGKATG KATGKDQAAA AAESKLLRDG
VAAAPAEDLV DLIEDLSEQM RNAAAELKFE LAGRLRDEIA DLKKELRRMK DAGHA
//
