(data stored in SCRATCH zone)

SWISSPROT: A4AVG0_MARSH

ID   A4AVG0_MARSH            Unreviewed;       663 AA.
AC   A4AVG0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081106};
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=FB2170_00910 {ECO:0000313|EMBL:EAR00182.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00182.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00182.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:SAAS01081113}.
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:SAAS01081110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01144535}.
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       ECO:0000256|SAAS:SAAS01081111}.
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DR   EMBL; CP002157; EAR00182.1; -; Genomic_DNA.
DR   RefSeq; WP_013304877.1; NC_014472.1.
DR   STRING; 313603.FB2170_00910; -.
DR   EnsemblBacteria; EAR00182; EAR00182; FB2170_00910.
DR   KEGG; fbc:FB2170_00910; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; MSP313603:G1GNS-448-MONOMER; -.
DR   Proteomes; UP000001602; 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   CDD; cd00079; HELICc; 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   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;
DR   PRODOM; A4AVG0.
DR   SWISS-2DPAGE; A4AVG0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01144540}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01144521};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01144538};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081119};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01144510};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081136};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01144519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081129}.
FT   DOMAIN       24    161       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      429    591       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   DOMAIN      626    661       UVR. {ECO:0000259|PROSITE:PS50151}.
FT   NP_BIND      37     44       ATP. {ECO:0000256|HAMAP-Rule:MF_00204}.
FT   COILED      427    447       {ECO:0000256|SAM:Coils}.
FT   COILED      622    649       {ECO:0000256|SAM:Coils}.
FT   MOTIF        90    113       Beta-hairpin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00204}.
SQ   SEQUENCE   663 AA;  76313 MW;  12F61BD29AA61B77 CRC64;
     MKFKVVSEFK PTGDQPEAIR QLEEGINSQE PYQTLLGVTG SGKTFSVANV IEKVQRPTLV
     LAHNKTLAAQ LYSEFKQFFP NNAVEYFVSY YDYYQPEAYI PTSGLYIEKD LSINEDIEKL
     RLSATSSLLS GRRDVLVVAS VSCLYGIGNP VEFQKNVISI FKNQVIARTK LLHMLVQSLY
     SRTTADFRNG NFRVKGDVVD VFPSYADHAF RIHFFGDEIE EIEAFDPFNN NVIEVYENLN
     IYPANMFVTS PDILQNAIHY IQDDLVHQID YFKEIGKPLE AKRLEERTNF DLEMIRELGY
     CSGIENYSRY LDGREPGTRP FCLLDYFPDD YLMVIDESHV TIPQVHAMYG GDRSRKENLV
     EYGFRLPAAM DNRPLKFEEF EALQNQVIYV SATPADYELQ LCQGVYVEQV IRPTGLLDPI
     IEVRPSLNQI DDLVEEIQQR VEKDERTLVT TLTKRMAEEL TKYLSRINVR CRYIHSDVDT
     LERVEIMQDL RKGIFDVLIG VNLLREGLDL PEVSLVAILD ADKEGFLRSN RSLTQTVGRA
     ARHLNGKAIM YADKITASMQ KTIDETNYRR EKQIAYNTAN NVTPKALNKS LDSVLAKNSV
     STYHFEKEEL RAAEPDMDYL TKEQIEKMIR DKRKAMEKAA KELDFMQAAK LRDEIKMLQN
     QDK
//

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