GenomeNet

Database: UniProt
Entry: M9RCG1_9RHOB
LinkDB: M9RCG1_9RHOB
Original site: M9RCG1_9RHOB 
ID   M9RCG1_9RHOB            Unreviewed;       735 AA.
AC   M9RCG1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
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:AGI69443.1};
GN   ORFNames=OAN307_c40230 {ECO:0000313|EMBL:AGI69443.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI69443.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI69443.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI69443.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003740; AGI69443.1; -; Genomic_DNA.
DR   RefSeq; WP_015501378.1; NC_020911.1.
DR   AlphaFoldDB; M9RCG1; -.
DR   STRING; 391626.OAN307_c40230; -.
DR   KEGG; oat:OAN307_c40230; -.
DR   eggNOG; COG0556; Bacteria.
DR   HOGENOM; CLU_009621_2_1_5; -.
DR   OrthoDB; 9806651at2; -.
DR   Proteomes; UP000005307; 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}; 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|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00204}.
FT   DOMAIN          55..187
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          460..626
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          652..687
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           121..144
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   735 AA;  82996 MW;  804243E4D60AF14C CRC64;
     MPYAQTDKSE AEQFLANPAP DVKTREKLEG GRAFVLKTEF EPAGDQPTAI KELCEGIRNG
     ERDQVLLGAT GTGKTFTMAK MIEETQRPAI ILAPNKTLAA QLYGEFKSFF PEAAVEYFVS
     FYDYYQPEAY VARSDTFIEK ESQINEQIDR MRHSATRSLL ERDDVIIVAS VSCIYGIGSV
     ETYGAMTQDL HTGEEYNQRQ IMADLIAQAY KRNDAGFQRG TFRVRGDSLE VWPAHLDDRA
     WKLSFFGEEL EAITEFDPLT GEKTDTFEKV RIYANSHYVT PKPTMKQAVV GIKKELRMRL
     DQFVSEGKLL EAQRLEQRCN FDLEMLEATG VCNGIENYSR YLTGRMPGEP PPTLFEFIPD
     NAIVFADESH VSVPQIGGMY KGDFRRKMTL AEHGFRLPSC MDNRPLKFEE WDAMRPQSVF
     VSATPAAWEM EQTGGVFTEQ IIRPTGLIDP MIEIRPVETQ VDDVMDEIRR VSAKGFRTLV
     TTLTKRMAED LTEYLHENGI KVRYMHSDID TIERIEILRD LRLGAFDVLI GINLLREGLD
     IPECGLVAIL DADKEGFLRS ETSLIQTIGR AARNAEGRVI MYADRITGSM ERAMGETDRR
     RDRQIAYNEK HGITPTTVKK NVEDILAGLY KGDVDMNRVT ATIDTPAGPN LKAVLDGLRV
     DMRKAAENLE FEEAARLRDE VKRLETVDLM VSDNPMARQY QVDKAVKESK KQAGRSTAGQ
     PGQRGGVKPR KKRGG
//
DBGET integrated database retrieval system