ID A0A1U7CTF3_9BACT Unreviewed; 686 AA.
AC A0A1U7CTF3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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_2 {ECO:0000313|EMBL:APW62230.1};
GN Synonyms=uvrB {ECO:0000256|HAMAP-Rule:MF_00204};
GN ORFNames=BSF38_03766 {ECO:0000313|EMBL:APW62230.1};
OS Paludisphaera borealis.
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Paludisphaera.
OX NCBI_TaxID=1387353 {ECO:0000313|EMBL:APW62230.1, ECO:0000313|Proteomes:UP000186309};
RN [1] {ECO:0000313|Proteomes:UP000186309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX4 {ECO:0000313|Proteomes:UP000186309};
RA Ivanova A.;
RT "Comparative genomics of four Isosphaeraceae planctomycetes: a common pool
RT of plasmids and glycoside hydrolase genes.";
RL Submitted (DEC-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}.
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DR EMBL; CP019082; APW62230.1; -; Genomic_DNA.
DR RefSeq; WP_076348180.1; NZ_CP019082.1.
DR AlphaFoldDB; A0A1U7CTF3; -.
DR STRING; 1387353.BSF38_03766; -.
DR KEGG; pbor:BSF38_03766; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000186309; 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; 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}; 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:UP000186309};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 25..173
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 429..595
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 619..654
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 652..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..114
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 686 AA; 76957 MW; 6291BA7E53C1F287 CRC64;
MSEYQLVSPY QPAGDQPQAI DELVKGLADG RASQTLMGVT GSGKTFTMAN VIAQYGKPAL
VMSHNKTLAA QLYAEFKEFF PHNAVRYFVS YYDYYQPEAY IPQRDIYIEK DASINEEIER
LRLASTSALV SRQDVIVVAS VSCIYGLGSP DDYRKMMVRL KVGDLVDRDE LLLKFVDIQY
DRNDVSFERG KFRVRGDVIE LWPAYEEFGF RIELFGDEVE RLATIDGLTG SVLETHQDLY
VYPAKHFVLP EERIQGAVAA IGNELEERLQ TLKEQGKLLE AQRLAARTRY DMEMLLEVGY
CSGIENYSRH LSGRKAGETP NTLLDFFPPD SLLILDESHV SLPQIRGMFA GDHSRKLTLV
EHGFRLPSAL DNRPLRIDEW ESKPARRLFV SATPGDYEVT MSGGEVVEQV IRPTGLIDPV
VRVEPARGQV PALLEEAKKR AAKGERVLVT TLTKRLAEDL TRYLKEQGLR CKWLHSELDA
IERMTILREL REGAFDVLVG VNLLREGLDL PEVSMVCILD ADKEGFLRSE TSLIQTIGRS
ARHVNAEVVL YADRITNSMQ RAMDETERRR VLQTAYNAEH GITPESVVKA IRRGIEEEIQ
ARTVAREAVG RDEATDATEE YLDALEGEML DAAEKLEFER AAALRDKIQQ LRAAQGGGSA
RPAPSPQGQS AKAKAKAKAR AGKKRG
//
