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Database: UniProt
Entry: Q9HMT9
LinkDB: Q9HMT9
Original site: Q9HMT9 
ID   UVRB_HALSA              Reviewed;         689 AA.
AC   Q9HMT9;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   31-JUL-2019, entry version 107.
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};
GN   OrderedLocusNames=VNG_2390G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales; Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M.,
RA   Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J.,
RA   Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A.,
RA   Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W.,
RA   Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H.,
RA   Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H.,
RA   Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D.,
RA   Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. A damage recognition complex composed
CC       of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC       binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC       DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC       binding by UvrB and probably causes local melting of the DNA
CC       helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC       strands. Then UvrB probes one DNA strand for the presence of a
CC       lesion. If a lesion is found the UvrA subunits dissociate and the
CC       UvrB-DNA preincision complex is formed. This complex is
CC       subsequently bound by UvrC and the second UvrB is released. If no
CC       lesion is found, the DNA wraps around the other UvrB subunit that
CC       will check the other stand for damage. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; AE004437; AAG20482.1; -; Genomic_DNA.
DR   PIR; F84389; F84389.
DR   RefSeq; WP_010903784.1; NC_002607.1.
DR   SMR; Q9HMT9; -.
DR   PaxDb; Q9HMT9; -.
DR   EnsemblBacteria; AAG20482; AAG20482; VNG_2390G.
DR   GeneID; 5953365; -.
DR   KEGG; hal:VNG_2390G; -.
DR   PATRIC; fig|64091.14.peg.1850; -.
DR   eggNOG; arCOG04748; Archaea.
DR   eggNOG; COG0556; LUCA.
DR   InParanoid; Q9HMT9; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 4923at2157; -.
DR   PhylomeDB; Q9HMT9; -.
DR   Proteomes; UP000000554; 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:ATPase 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   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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN         1    689       UvrABC system protein B.
FT                                /FTId=PRO_0000138453.
FT   DOMAIN       40    422       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      443    605       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      632    667       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF       106    129       Beta-hairpin.
SQ   SEQUENCE   689 AA;  77507 MW;  BED16C96A94E93B8 CRC64;
     MSDASGPLQP DRPEADVPFR VEAPFDPAGD QPDAIAELVA GYEQGAQQQT LLGVTGSGKT
     NTVSWVVEEL QQPTLVIAHN KTLAAQLYEE FRSLFPDNAV EYFVSYYNYY QPEAYVEQTD
     KYIEKDASIN DEIDRLRHSA TRSLLTRDDV IVVASVSAIY GLGDPRNYEE MSLRVERGQS
     IGRDQLLAKL VDLNYDRNDV DFTQGTFRVR GDTVEVYPMY GRYPVRVEFW GDEIDRMAKL
     DPLEGTVESE EPAVLFHPAE HYSVPDAEME QAIERIRTDM HERVRHFERT GDMVAAQRIE
     ERTTFDLEMM AEAGYCSGIE NYSVYLSDRE VGDAPYTLLD YFPDDFLTVI DESHRTVPQI
     KGQYEGDKSR KDSLVDNGFR LPTAYDNRPL TFAEFADKTD RTLYVSATPG DHERAQSANV
     VEQIVRPTHL VDPDISIADA TGQVEDLMDR IDERVARDER VLVTTLTKRM AEDLTEYLEE
     AGVAVEYMHD ETDTLERHEL VRGLRLGEYD VLVGINLLRE GLDIPEVSLV AILDADQQGF
     LRSETSLVQT MGRAARNVNG EVVLYADETT DAMQAAIDET QRRRRIQRAF NEDHGTTPTT
     IEKAVGDMNL PGAETDTADV AGDAPSDEQE AALLVEDLEA RMEDAASNLE FELAADIRDR
     MRELREAFDL DGGDAPEDPG GVAPETEDW
//
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