UVRA_SALTY
ID UVRA_SALTY Reviewed; 941 AA.
AC P0A195; P37434;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=STM4254;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NM522;
RA Alberti M., Li Y.F., Sancar A., Hearst J.E.;
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; M93014; AAA27250.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23078.1; -; Genomic_DNA.
DR RefSeq; NP_463119.1; NC_003197.2.
DR RefSeq; WP_000357724.1; NC_003197.2.
DR AlphaFoldDB; P0A195; -.
DR SMR; P0A195; -.
DR STRING; 99287.STM4254; -.
DR PaxDb; P0A195; -.
DR PRIDE; P0A195; -.
DR EnsemblBacteria; AAL23078; AAL23078; STM4254.
DR GeneID; 1255780; -.
DR KEGG; stm:STM4254; -.
DR PATRIC; fig|99287.12.peg.4474; -.
DR HOGENOM; CLU_001370_0_2_6; -.
DR OMA; PFEGIIP; -.
DR PhylomeDB; P0A195; -.
DR BioCyc; SENT99287:STM4254-MON; -.
DR Proteomes; UP000001014; 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; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..941
FT /note="UvrABC system protein A"
FT /id="PRO_0000093086"
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 BINDING 640..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
SQ SEQUENCE 941 AA; 103928 MW; C4AFC9F549060C26 CRC64;
MDKIEVRGAR THNLKNINLV IPRDKLIVVT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT ITEIHDYLRL LFARVGEPRC
PDHDVPLAAQ TVSQMVDNVL SQPEGKRLML LAPIIKERKG EHTKTLENLA SQGYIRARID
GEVCDLSDPP KLELQKKHTI EVVIDRFKVR NDLSQRLAES FETALELSGG TAVVADMDDE
KAEELLFSAN FACPICGYSM RELEPRLFSF NNPAGACPTC DGLGVQQYFD PDRVIQNPDL
SLAGGAIRGW DRRNFYYFQM LKSLAEHYKF DVDAPWASLS ANVHKVVLYG SGKENIEFKY
MNDRGDTSVR RHPFEGVLHN MERRYKETES SAVREELAKF ISNRPCASCE GTRLNREARH
VFVENTPLPA ISDMSIGHAM DFFTNLKLSG QRAKIAEKVL KEIGDRLKFL VNVGLNYLTL
SRSAETLSGG EAQRIRLASQ IGAGLVGVMY VLDEPSIGLH QRDNERLLGT LIHLRNLGNT
VIVVEHDEDA IRAADHVIDI GPGAGVHGGE VVAEGPLEAI MAVPESLTGQ YMSGKRKIEV
PKQRVPANPE KVLKLTGARG NNLKDVTLTL PVGLFTCITG VSGSGKSTLI NDTLFPIAQR
QLNGATIAEP APYRDIQGLE HFDKVIDIDQ SPIGRTPRSN PATYTGVFTP VRELFAGVPE
SRSRGYTPGR FSFNVRGGRC EACQGDGVIK VEMHFLPDIY VPCDQCKGKR YNRETLEIKY
KGKTIHEVLD MTIEEAREFF DAVPALARKL QTLMDVGLTY IRLGQSATTL SGGEAQRVKL
ARELSKRGTG QTLYILDEPT TGLHFADIQQ LLDVLHQLRD QGNTIVVIEH NLDVIKTADW
IVDLGPEGGS GGGEILVAGT PETVAECEAS HTARFLKPML K
