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Database: UniProt/TrEMBL
Entry: D2B9S4_STRRD
LinkDB: D2B9S4_STRRD
Original site: D2B9S4_STRRD 
ID   D2B9S4_STRRD            Unreviewed;       711 AA.
AC   D2B9S4;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   26-NOV-2014, entry version 41.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|SAAS:SAAS00088419};
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   OrderedLocusNames=Sros_2983 {ECO:0000313|EMBL:ACZ85937.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 /
OS   NI 9100).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ85937.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A.,
RA   Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100T).";
RL   Stand. Genomic Sci. 2:29-37(2010).
RN   [2] {ECO:0000313|EMBL:ACZ85937.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A.,
RA   Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.-F.,
RA   Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Land M., Hauser L., Chang Y.-J., Jeffries C.D.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Chain P., Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
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:0000256|HAMAP-
CC       Rule:MF_00204, ECO:0000256|SAAS:SAAS00088361}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
CC       ECO:0000256|SAAS:SAAS00088351}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00088404}.
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|HAMAP-
CC       Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
CC   -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000256|HAMAP-
CC       Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000256|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000256|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Contains UVR domain. {ECO:0000256|SAAS:SAAS00088408}.
CC   -!- SIMILARITY: Contains helicase ATP-binding domain.
CC       {ECO:0000256|SAAS:SAAS00088346}.
CC   -!- SIMILARITY: Contains helicase C-terminal domain.
CC       {ECO:0000256|SAAS:SAAS00088426}.
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DR   EMBL; CP001814; ACZ85937.1; -; Genomic_DNA.
DR   RefSeq; YP_003338680.1; NC_013595.1.
DR   ProteinModelPortal; D2B9S4; -.
DR   EnsemblBacteria; ACZ85937; ACZ85937; Sros_2983.
DR   GeneID; 8666270; -.
DR   KEGG; sro:Sros_2983; -.
DR   PATRIC; 32467943; VBIStrRos112010_2964.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; GIAGWHE; -.
DR   OrthoDB; EOG6B360R; -.
DR   BioCyc; SROS479432:GI0V-3006-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 4.
DR   Gene3D; 4.10.860.10; -; 1.
DR   HAMAP; MF_00204; UvrB; 1.
DR   InterPro; IPR006935; Helicase/UvrB_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR004807; UvrB.
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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
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 {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU004294};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002029};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS00088343};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_00204};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00204};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU004294};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587}.
FT   DOMAIN      447    613       Helicase C-terminal. {ECO:0000256|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      666    701       UVR. {ECO:0000256|HAMAP-Rule:MF_00204}.
FT   NP_BIND      56     63       ATP. {ECO:0000256|HAMAP-Rule:MF_00204}.
FT   MOTIF       109    132       Beta-hairpin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00204}.
SQ   SEQUENCE   711 AA;  80361 MW;  6DD47D52EE4B9E16 CRC64;
     MAPPTVGGVR PVTDLQRKVA PFEVVTDMTP SGDQPTAIAE LERRVKAGDK DNVLLGATGT
     GKTATVAWLI ERLQRPTLVI QPNKTLAAQF ANELREMMPN NAIEYFVSYY DYYQPEAYVP
     QSDTYIEKDS SINDEVERLR HSATNSLLTR RDTIVVASVS CIYGLGTPQE YVDRMTSLKV
     GQEIERDSLL RRLVDMQYTR NDLAFTRGTF RVRGDTIEII PKYEELAVRI EMFGDEIEKL
     STMHPLTGEV ITEDEELYIF PASHYVAGTE RMEKAVRGIE AELAQTLETM ERQGKLLEAQ
     RLRMRTTYDL EMMRQIGTCS GIENYSRHMD GRAPGSAPNT LLDYFPEDFL LVLDESHQTV
     PQIGAMYEGD ASRKRTLVEH GFRLPSAMDN RPLKWEEFLE RIDQTVYLSA TPGTYELGRS
     KGDVVEQVIR PTGLVDPEVI VKPTKSQIDD LVHEIRTRTE KDERVLVTTL TKKMSEDLTD
     YLLELGIRVR YLHSEVDTLR RIELLRELRM GEFDVLVGIN LLREGLDLPE VSLVAILDAD
     KEGFLRSETS LIQTIGRAAR NVSGQVHMYA DRITPSMERA IEETNRRRAK QTAYNEANGI
     DPQPLRKKIA DILDSLNRED ADTAQLLGGS GRQQSRGKAP VPGFVVKQVG QHAKAIAGEM
     PRAQLEALVE SLTDQMHQAA TDLQFEVAAR LRDEIKELKR EVRDMREAGV S
//
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