ID Q4C810_CROWT Unreviewed; 680 AA.
AC Q4C810;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 99.
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=CwatDRAFT_5490 {ECO:0000313|EMBL:EAM52461.1};
OS Crocosphaera watsonii WH 8501.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM52461.1, ECO:0000313|Proteomes:UP000003922};
RN [1] {ECO:0000313|EMBL:EAM52461.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM52461.1,
RC ECO:0000313|Proteomes:UP000003922};
RG DOE Joint Genome Institute;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAM52461.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM52461.1,
RC ECO:0000313|Proteomes:UP000003922};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M.;
RT "Annotation of the draft genome assembly of Crocosphaera watsonii WH
RT 8501.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAM52461.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM52461.1,
RC ECO:0000313|Proteomes:UP000003922};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Crocosphaera watsonii WH
RT 8501.";
RL Submitted (JUN-2005) 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:EAM52461.1}.
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; AADV02000002; EAM52461.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4C810; -.
DR KEGG; cwa:CwatDRAFT_5490; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000003922; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003922};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW ECO:0000256|RuleBase:RU003587}.
FT DOMAIN 39..192
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 443..605
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 640..675
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 636..675
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 105..128
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 52..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 680 AA; 78042 MW; D131E0945094A26A CRC64;
MLALQNCLLF LMMTNPIFNL KAPFKPTGDQ PSAIKQLTKS IEAGNRFQTL LGATGTGKTF
SVAAVIENIG KPTLVLAHNK TLAAQLCNEF RQFFPNNAVE YFISYYDYYQ PEAYIPVSDT
YIEKTASIND EIDMLRHSAT RSLFERKDVI VVASISCIYG LGMPSEYLKA SVPLVVGKEV
DQRQLLRDLV TIQYSRNDLE LQRGRFRVKG DVLEIVPAYE DRVIRVEFFG DEIDAIRYLD
PVTGDILNSL KNINIYPARH FVTPDEQLEF ACEAIDIELK QQVQCLEKAG KLLELQRINQ
RTRYDLELLR EVGYCNGVEN YSRHLAGRKA GSPPECLVDY FPRDWLLIVD ESHVTVPQIR
GMYNGDQARK KVLIDHGFRL PSAADNRPLK SEEFWDKVNQ CIFVSATPGN WEIEQSEERV
IEQIIRPTGV LDPEIFVRPT EGQVDDLLGE IKQRVKRQER VLITTLTKRM SEDLTEYFQE
RDIKVRYLHS EIKSIERIEI LQALRNGEFD VLIGVNLLRE GLDLPEVSLV AILDADKEGF
LRAEKSLIQT IGRAARHVNG QAILYGDNLT DSMIKAMEET ERRRNIQMAH NKRHNITPKP
IIKRSSNAIL SFLDISRRLN SQELEEVYTQ ADDLPLDKVP ELIQQLEQQM QEAAKNLEFE
EAAKYRDKIK RLRDKILGHK
//