UVRB_PROMM
ID UVRB_PROMM Reviewed; 679 AA.
AC Q7TV80;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204};
DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204};
DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204};
GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; OrderedLocusNames=PMT_0071;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP-
CC Rule:MF_00204}.
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DR EMBL; BX548175; CAE20246.1; -; Genomic_DNA.
DR RefSeq; WP_011129450.1; NC_005071.1.
DR AlphaFoldDB; Q7TV80; -.
DR SMR; Q7TV80; -.
DR STRING; 74547.PMT_0071; -.
DR PRIDE; Q7TV80; -.
DR EnsemblBacteria; CAE20246; CAE20246; PMT_0071.
DR KEGG; pmt:PMT_0071; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_3; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000001423; 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 Gene3D; 3.40.50.300; -; 3.
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 PANTHER; PTHR24029; PTHR24029; 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; SSF46600; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00631; uvrb; 1.
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; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..679
FT /note="UvrABC system protein B"
FT /id="PRO_0000227342"
FT DOMAIN 25..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 429..591
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 639..674
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 91..114
FT /note="Beta-hairpin"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 679 AA; 76869 MW; 68AB3227DD031387 CRC64;
MPKYHLKAPY SPKGDQPTAI ARLVEGVNQG QRYQTLLGAT GTGKTFTIAN LIAQTGRPAL
VLAHNKTLAA QLCNEFREFF PDNSVEYFIS YYDYYQPEAY VPVSDTYIAK TSSINEEIDM
LRHSATRSLF ERNDVIVVAS ISCIYGLGIP SEYLKAAVKF KVGETLNIRS ALRELVENQY
SRNDIDITRG RFRVRGDVLE IGPAYEDRLV RIELFGDEVE AIRYLDPTTG EILQSLEAIN
IYPAKHFVTP KERLNVAVQA IRDELRGRLQ FLNEQGKLLE AQRLEQRTTY DLEMLREVGY
CNGVENYARH LAGRSAGTPP ECLIDYFPED WLLVVDESHV TCSQLKAMYN GDQARKKVLI
EHGFRLPSAA DNRPLKSEEF WSKARQTVFV SATPGDWELK QSDGHLAEQV IRPTGVLDPL
VEVRPTQGQV DDLLAEIRIR AEKQERVLIT TLTKRMAEDL TDYLAENDVR VRYLHSEIHS
IERIEIIQDL RLGEYDVLVG VNLLREGLDL PEVSLVVILD ADKEGFLRAE RSLIQTIGRA
ARHVDGMALL YADNLTDSMS RAISETERRR EIQKAYNELN GIVPRPAGKR ASNSILSFLE
LSRRLQTDGK DADLVQITGR AVDALDSDQD AGLALDALPE LIDQLETKMK EAAKNLNFEE
AASLRDRIKK FRQKLIRNT
