ID UVRA_SHIFL Reviewed; 940 AA.
AC P0A699; P07671; P76788;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 27-MAR-2024, entry version 123.
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}; Synonyms=dinE;
GN OrderedLocusNames=SF4146, S3583;
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- MISCELLANEOUS: Binds about 2 zinc atoms/molecule. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; AE005674; AAN45568.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18629.1; -; Genomic_DNA.
DR RefSeq; NP_709861.1; NC_004337.2.
DR RefSeq; WP_000357740.1; NZ_WPGW01000193.1.
DR AlphaFoldDB; P0A699; -.
DR SMR; P0A699; -.
DR STRING; 198214.SF4146; -.
DR PaxDb; 198214-SF4146; -.
DR GeneID; 1027393; -.
DR GeneID; 75204201; -.
DR KEGG; sfl:SF4146; -.
DR KEGG; sfx:S3583; -.
DR PATRIC; fig|198214.7.peg.4893; -.
DR HOGENOM; CLU_001370_0_2_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 CDD; cd03270; ABC_UvrA_I; 1.
DR CDD; cd03271; ABC_UvrA_II; 1.
DR Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00630; uvra; 1.
DR PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1.
DR PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..940
FT /note="UvrABC system protein A"
FT /id="PRO_0000093088"
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; 103868 MW; D61AAEB6514B860C CRC64;
MDKIEVRGAR THNLKNINLV IPRDKLIVVT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT ITEIHDYLRL LFARVGEPRC
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
//
