UVRA_ECO27
ID UVRA_ECO27 Reviewed; 940 AA.
AC B7UPM7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 89.
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, ECO:0000312|EMBL:CAS11930.1};
GN OrderedLocusNames=E2348C_4382 {ECO:0000312|EMBL:CAS11930.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1] {ECO:0000312|EMBL:CAS11930.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=32023456; DOI=10.1016/j.celrep.2020.01.014;
RA Lawaree E., Jankevicius G., Cooper C., Ahel I., Uphoff S., Tang C.M.;
RT "DNA ADP-Ribosylation Stalls Replication and Is Reversed by RecF-Mediated
RT Homologous Recombination and Nucleotide Excision Repair.";
RL Cell Rep. 30:1373-1384(2020).
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 -!- FUNCTION: Plays a role in recovery after DNA ADP-ribosylation.
CC {ECO:0000269|PubMed:32023456}.
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 -!- DISRUPTION PHENOTYPE: Significantly reduced survival of cells
CC expressing DNA ADP-ribosyl transferase (darT) mutant G49D.
CC {ECO:0000269|PubMed:32023456}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; FM180568; CAS11930.1; -; Genomic_DNA.
DR RefSeq; WP_000357763.1; NC_011601.1.
DR SMR; B7UPM7; -.
DR EnsemblBacteria; CAS11930; CAS11930; E2348C_4382.
DR KEGG; ecg:E2348C_4382; -.
DR HOGENOM; CLU_001370_0_2_6; -.
DR OMA; RAGEPHC; -.
DR Proteomes; UP000008205; 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: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; 1.
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_0000456043"
FT DOMAIN 310..587
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 607..937
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 253..280
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 740..766
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 640..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 940 AA; 103884 MW; A20C90C935A0ACEB CRC64;
MDKIEVRGAR THNLKNINLV IPRDKLIVVT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT ITEIHDYLRL LYARVGEPRC
PDHDVPLAAQ TVSQMVDNVL SQPEGKRLML LAPIIKERKG EHTKTLENLA SQGYIRARID
GEVCDLSDPP KLELQKKHTI EVVVDRFKVR DDLTQRLAES FETALELSGG TAVVADMDDP
KAEELLFSAN FACPICGYSM RELEPRLFSF NNPAGACPTC DGLGVQQYFD PDRVIQNPEL
SLAGGAIRGW DRRNFYYFQM LKSLADHYKF DVEAPWGSLS ANVHKVVLYG SGKENIEFKY
MNDRGDTSIR RHPFEGVLHN MERRYKETES SAVREELAKF ISNRPCASCE GTRLRREARH
VYVENTPLPA ISDMSIGHAM EFFNNLKLAG QRAKIAEKIL KEIGDRLKFL VNVGLNYLTL
SRSAETLSGG EAQRIRLASQ IGAGLVGVMY VLDEPSIGLH QRDNERLLGT LIHLRDLGNT
VIVVEHDEDA IRAADHVIDI GPGAGVHGGE VVAEGPLEAI MAVPESLTGQ YMSGKRKIEV
PKKRVPANPE KVLKLTGARG NNLKDVTLTL PVGLFTCITG VSGSGKSTLI NDTLFPIAQR
QLNGATIAEP APYRDIQGLE HFDKVIDIDQ SPIGRTPRSN PATYTGVFTP VRELFAGVPE
SRARGYTPGR FSFNVRGGRC EACQGDGVIK VEMHFLPDIY VPCDQCKGKR YNRETLEIKY
KGKTIHEVLD MTIEEAREFF DAVPALARKL QTLMDVGLTY IRLGQSATTL SGGEAQRVKL
ARELSKRGTG QTLYILDEPT TGLHFADIQQ LLDVLHKLRD QGNTIVVIEH NLDVIKTADW
IVDLGPEGGS GGGEILVSGT PETVAECEAS HTARFLKPML
