ID C6E8Y5_GEOSM Unreviewed; 947 AA.
AC C6E8Y5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=UvrABC system protein A;
DE Short=UvrA protein;
DE AltName: Full=Excinuclease ABC subunit A;
GN Name=uvrA; OrderedLocusNames=GM21_0189;
OS Geobacter sp. (strain M21).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC lesions (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA
CC family.
CC -!- SIMILARITY: Contains 2 ABC transporter domains.
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DR EMBL; CP001661; ACT16274.1; -; Genomic_DNA.
DR RefSeq; YP_003020032.1; NC_012918.1.
DR STRING; 443144.GM21_0189; -.
DR EnsemblBacteria; ACT16274; ACT16274; GM21_0189.
DR GeneID; 8135492; -.
DR KEGG; gem:GM21_0189; -.
DR PATRIC; 22014880; VBIGeoSp56140_0196.
DR eggNOG; COG0178; -.
DR HOGENOM; HOG000050449; -.
DR KO; K03701; -.
DR OMA; GAIKGWD; -.
DR ProtClustDB; CLSK829225; -.
DR BioCyc; GSP443144:GHKM-193-MONOMER; -.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:HAMAP.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:HAMAP.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR GO; GO:0006810; P:transport; IEA:HAMAP.
DR Gene3D; 3.30.1490.20; -; 2.
DR HAMAP; MF_00205; UvrA; 1; -.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004602; UvrA.
DR Pfam; PF00005; ABC_tran; 2.
DR TIGRFAMs; TIGR00630; uvra; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW Excision nuclease; Membrane; Metal-binding; Nucleotide-binding;
KW Repeat; SOS response; Transport; Zinc; Zinc-finger.
FT DOMAIN 334 600 ABC transporter 1 (By similarity).
FT DOMAIN 611 941 ABC transporter 2 (By similarity).
FT NP_BIND 33 40 ATP (By similarity).
FT ZN_FING 259 286 C4-type (By similarity).
FT NP_BIND 645 652 ATP (By similarity).
FT ZN_FING 744 770 C4-type (By similarity).
SQ SEQUENCE 947 AA; 104633 MW; 6329F183A6A5477C CRC64;
MATDKIIIKG ACEHNLKCID VEIPRDKLVV ITGISGSGKS TLAFDTIYAE GQRRYVESLS
AYARQFLEQM EKPDVESIEG LSPAISIEQK TTSKNPRSTV GTVTEIYDYL RLLFARIGKP
HCYNCGRIIT SQTVSQMVDQ IAALPQGAKL TLLSPIVRGR KGEYKKELTQ FRKDGFARVV
VDGETHDLSE EITLDKKKKH DIDIVVDRLV VKPGIEKRLA DSLETALSHA EGIVKVALTP
DADRGIKEET LLFSESAACI ECGISYPEMT PRMFSFNNPY GACPDCTGLG TRMYLDTNLV
VPDHDLTLAE GAVAPWETRF SGWYQQTLAA LGKSYGFDLH TPYKQLSKKA KDVILNGSGG
ELVDFWWVDD AGKRHTYKKA FEGVLNNLER RHRETESEQV REELEKYMDV MPCPTCQGAR
LKKEALFVRV GGENIQQVTA YSIQDALSFF DSLALSEKEE DIARRILKEI RERLNFLVNV
GLDYLSLDRS SGTLSGGEGQ RIRLATQIGS SLVGVLYILD EPSIGLHQRD NGRLLSTLRH
LRDIGNTVLV VEHDEETISE ADWVIDMGPG AGVHGGEVVA EGTPAEIMAN PHSLTGRYLS
GALTIAIPKK RRKGSRFLSI EGANENNLKD VSVDLPLGVM TCITGVSGSG KSSLIIDTLY
KTLNQRLYKS REKAGAVRAI HGMEVLDKVI NIDQSPIGRT PRSNPATYTG LFTEIREIFA
QLPESKMRGY KPGRYSFNVK GGRCEACAGD GIIKIEMHFL PDVYVQCEVC KGARYNRETL
EVRFKGRSIA EVLDMTVSQA LVFLEHIPRL KAKLQTLEEV GLGYIKLGQS ATTLSGGEAQ
RVKLAKELSK RATGRTIYIL DEPTTGLHFA DIAKLLEVLH KLVDAGNSIV VIEHNLDVIK
TADWIVDLGP EGGDRGGEVI AVGTPEQVSR VERSYTGQYL KKMLPHG
//
