UVRB_PARUW
ID UVRB_PARUW Reviewed; 673 AA.
AC Q6MEV1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=pc0174;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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; BX908798; CAF22898.1; -; Genomic_DNA.
DR RefSeq; WP_011174724.1; NC_005861.1.
DR AlphaFoldDB; Q6MEV1; -.
DR SMR; Q6MEV1; -.
DR STRING; 264201.pc0174; -.
DR EnsemblBacteria; CAF22898; CAF22898; PC_RS00855.
DR KEGG; pcu:PC_RS00855; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_0; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000000529; 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..673
FT /note="UvrABC system protein B"
FT /id="PRO_0000227337"
FT DOMAIN 28..414
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 433..595
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 633..668
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 94..117
FT /note="Beta-hairpin"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 673 AA; 77789 MW; 2A9BA0C948B94539 CRC64;
MNPSQLFQLH TEFEPCGDQP EAINQLVASI LQNKRSQVLL GITGSGKTFT MANVIAKVQR
PTLILAHNKT LAAQLYQEFK AFFPHNAVEY FVSYYDYYQP EAYVPRTDTY IEKDMSINDK
IDKMRLSATR SLLERSDVII VSSVSCIYGL GSPEYYRGMN LTLSQGQMRR RDDILLHLVE
MQYKRNDFEF IRSTFRVRGD VLDIFPAYEE DLAIRVEMFG DEIEQISEID PLTGKVKRRI
ASITIYPSSH HVTPEEIRLK AMETIRAELD ERRQFYETEK KYLELERIQQ RTMYDLEMLK
EVGTCKGIEN YSRHFSMRQP GAPPPCLLDY FPSDYLLVID ESHQTLPQVH AMFNGDRARK
QTLVDFGFRL PSAFDNRPLR FEEVYGRIHQ VVYVSATPGA WEVQEAGGEI VEQLIRPTGL
LDPIIEIRPA SGQVDDCLAE IRSHVSKGGR VLLTTLTKKL SEELTTYLND LNVKAKYLHS
DIDTIERVQI IRDLRLGVFD VLVGINLLRE GLDIPEVSLV AILDADKEGF LRSETSLIQT
CGRAARNAEG RVIMYADKIT KSIKRTLEIT ESRRALQMRY NEQHGITPRT VKREISVLME
SEEDQVTHPT KLEEEIFKAA EEAHHYLTLD EVRLKIKECE KEMKKAAKEF RFEEAADWRD
QMRRYQQIEL TLA
