UVRA_VIBVU
ID UVRA_VIBVU Reviewed; 940 AA.
AC Q8DCJ3;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205};
DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205};
DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205};
GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; OrderedLocusNames=VV1_1427;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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 protein.
CC A damage recognition complex composed of 2 UvrA and 2 UvrB subunits
CC scans DNA for abnormalities. When the presence of a lesion has been
CC verified by UvrB, the UvrA molecules dissociate. {ECO:0000255|HAMAP-
CC Rule:MF_00205}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; AE016795; AAO09867.1; -; Genomic_DNA.
DR RefSeq; WP_011079386.1; NC_004459.3.
DR AlphaFoldDB; Q8DCJ3; -.
DR SMR; Q8DCJ3; -.
DR EnsemblBacteria; AAO09867; AAO09867; VV1_1427.
DR KEGG; vvu:VV1_1427; -.
DR HOGENOM; CLU_001370_0_2_6; -.
DR OMA; PFEGIIP; -.
DR Proteomes; UP000002275; 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:ATP hydrolysis 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 Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004602; UvrA.
DR InterPro; IPR041552; UvrA_DNA-bd.
DR InterPro; IPR041102; UvrA_inter.
DR Pfam; PF00005; ABC_tran; 1.
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; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW Excision nuclease; Metal-binding; Nucleotide-binding; Repeat; SOS response;
KW Zinc; Zinc-finger.
FT CHAIN 1..940
FT /note="UvrABC system protein A"
FT /id="PRO_0000093113"
FT DOMAIN 309..586
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 606..936
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 252..279
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 739..765
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 639..646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 940 AA; 103960 MW; 8DB4C3150866C40A CRC64;
MDKIEVRGAR THNLKNINLT IPRDKLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT ITEVYDYLRL LYARVGEPRC
PEHQVPLAAQ TISQMVDKVL ELPEGAKMML LAPIVKERKG EHVKTLENLA AQGFIRARID
GETCDLTDPP TLELHKKHTI EVVVDRVKVR GDLQQRLAES FETALELSGG IAVIAPMEGD
GEEIVFSANF ACPHCGYSMQ ELEPRLFSFN NPAGACGTCD GLGVQQYFDP ERVIQDANLS
LAQGAIRGWD QKNYYYFQML TSLAEHYDFD LHAPFNSLSK RIQEVILKGS GRTEIEFKYI
NDRGDIRLKR HPFEGILNTL ERRYRDTESN SVREELVKYI STKPCTSCGG TRLRLEARNV
FINDTTLPQI VELSIADALT FFATLKLEGQ RAQIAEKVMK EINDRLQFLV NVGLNYLNLS
RSAETLSGGE AQRIRLASQI GAGLVGVMYV LDEPSIGLHQ RDNERLLKTL THLRDLGNTV
LVVEHDEDAI RCADHVIDIG PGAGVHGGQV VAEGTMAEIL ANPDSLTGQY LSGAKQIIVP
TQRTPRDKNK TVELIGASGN NLKEVNLSVP VGLFSCITGV SGSGKSTLIN DTFFKIAHTQ
LNGATTAQPA PYKSIKGLEH FDKVIDIDQS PIGRTPRSNP ATYTGIFTPI RELFSGTQES
RSRGYKPGRF SFNVRGGRCE ACQGDGVIKV EMHFLPDVYV PCDVCKGKRY NRETLEVHYK
GKSIDEVLEM TVEDAHEFFA PVPVIARKLQ TLMDVGLSYI RLGQAATTLS GGEAQRVKLA
RELSKRDTGK TLYILDEPTT GLHFHDIQQL LTVLHRLRDH GNTVVVIEHN LDVIKTADWI
IDLGPEGGQG GGEIIAQGTP EDVAQIEGSH TARFLKPMLK