(data stored in ACNUC7421 zone)

SWISSPROT: Q145U8_PARXL

ID   Q145U8_PARXL            Unreviewed;       957 AA.
AC   Q145U8;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 107.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00088996};
DE            Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN   ORFNames=Bxe_A4108 {ECO:0000313|EMBL:ABE28891.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28891.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28891.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28891.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrA is an ATPase and a DNA-binding
CC       protein. A damage recognition complex composed of 2 UvrA and 2
CC       UvrB subunits scans DNA for abnormalities. When the presence of a
CC       lesion has been verified by UvrB, the UvrA molecules dissociate.
CC       {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00571360}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00571359}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00089096}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA
CC       family. {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00571366}.
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DR   EMBL; CP000270; ABE28891.1; -; Genomic_DNA.
DR   RefSeq; WP_011486720.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4108; -.
DR   EnsemblBacteria; ABE28891; ABE28891; Bxe_A4108.
DR   GeneID; 4005044; -.
DR   KEGG; bxb:DR64_1784; -.
DR   KEGG; bxe:Bxe_A4108; -.
DR   PATRIC; fig|266265.5.peg.375; -.
DR   eggNOG; ENOG4105C5U; Bacteria.
DR   eggNOG; COG0178; LUCA.
DR   HOGENOM; HOG000050448; -.
DR   KO; K03701; -.
DR   OMA; VIEMNFL; -.
DR   OrthoDB; 152379at2; -.
DR   BioCyc; BXEN266265:BXE_RS01775-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
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:0008270; F:zinc ion binding; 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_00205; UvrA; 1.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   InterPro; IPR041552; UvrA_DNA-bd.
DR   InterPro; IPR041102; UvrA_inter.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00630; uvra; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145U8.
DR   SWISS-2DPAGE; Q145U8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00461349};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461486};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461370};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461384};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00089139};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461351};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461435};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461425};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00461357};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461462};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00461396};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461452}.
FT   DOMAIN      610    947       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND      31     38       ATP. {ECO:0000256|HAMAP-Rule:MF_00205}.
FT   ZN_FING     261    288       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00205}.
FT   NP_BIND     651    658       ATP. {ECO:0000256|HAMAP-Rule:MF_00205,
FT                                ECO:0000256|PROSITE-ProRule:PRU00434}.
FT   ZN_FING     750    776       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00205}.
SQ   SEQUENCE   957 AA;  106126 MW;  596CC8BFA4AEB799 CRC64;
     MEQIRIRGAR THNLKNVNLD LPRHKLVVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLQLMEK PDVDLIEGLS PAISIEQKAT SHNPRSTVGT VTEIHDYLRL LFARVGTPYC
     PDHEIPLEAQ SVSQMVDAAL ALPDETKLMI LAPVVANRKG EHVELFEEMQ AQGFIRFRVR
     SGGGTANEGV AKIYEVDSLP KLKKNDKHTI DVVVDRLKVR PDMKQRLAES FETALRLADG
     RAIALEMDTD KEHLFSSKFA CPICSYSLQE LEPRLFSFNN PMGACPECDG LGQITFFDPK
     RVVAHPSLSL AAGAVKGWDR RNQFYFQMLQ SLAAFYEFDI DTAVEDLPEK VRKILLFGSG
     KQEIPFSYIN ERGRTSVREH VFEGIIPNLE RRYRETDSVA VREELAKYQN NQPCPACAGT
     RLRREARFVR IGTDSDARGI FEISGWPLRD ALGYFQTLRL EGSKREIADK VVKEIVARLM
     FLNNVGLDYL SLERSAETLS GGEAQRIRLA SQIGSGLTGV MYVLDEPSIG LHQRDNDRLI
     ATLKHLRDLG NSVIVVEHDE DMIRMADYVV DMGPGAGEHG GMVIAEGTPK QVQANAASMT
     GQYMSGARNI EFPDERKAPD ERRLRIVEAY GNNLKHVSLD LPVGLLTCVT GVSGSGKSTL
     INDTLYHAVA HHLYGSATEP APYESIEGLE HFDKVINVDQ SPIGRTPRSN PATYTGLFTP
     IRELFAGVPA AKERGYEAGR FSFNVKGGRC ESCQGDGVLK VEMHFLPDVY VPCDVCHGKR
     YNRETLDVQY KGRNISEVLD MTVENAYEFF KPVPVVARKL KTLLDVGLGY IRLGQSATTL
     SGGEAQRVKL SLELSKRDTG RTLYILDEPT TGLHFHDIAL LLEVIHRLRD QGNTVVIIEH
     NLDVIKTADW VIDLGPEGGA GGGQIVAQGT PEQVAKSKAS FTGKYLAPLL KRAASKK
//

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