UVRA_LEPIC
ID UVRA_LEPIC Reviewed; 948 AA.
AC Q72RM8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=LIC_11717;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS70306.1; -; Genomic_DNA.
DR RefSeq; WP_001156251.1; NC_005823.1.
DR AlphaFoldDB; Q72RM8; -.
DR SMR; Q72RM8; -.
DR PaxDb; Q72RM8; -.
DR EnsemblBacteria; AAS70306; AAS70306; LIC_11717.
DR GeneID; 61141613; -.
DR KEGG; lic:LIC_11717; -.
DR HOGENOM; CLU_001370_0_2_12; -.
DR OMA; PFEGIIP; -.
DR Proteomes; UP000007037; Chromosome I.
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; IPR003593; AAA+_ATPase.
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; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SMART; SM00382; AAA; 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..948
FT /note="UvrABC system protein A"
FT /id="PRO_0000093058"
FT DOMAIN 307..586
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 606..934
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 249..277
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 737..763
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 638..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 948 AA; 105536 MW; 7900372D53C5EF4D CRC64;
MQEIRIRGAR EHNLKNINVD IPRDQLVVIT GLSGSGKSSL AFDTIYAEGQ RRYVESLSAY
ARQFLGQMEK PDLDLIEGLS PAISIEQKTT HRNPRSTVGT VTEIYDYLRL LYARVGKPHC
PECGTPIQSM SIDQITARVL AFPQGSKLQI LAPVISGKKG EHKDVLEKIR KDGFNRVRIN
GEIRTLEEEI VLKKNFKTSI EIVVDRIVMK EGIRSRLADS VETALKQSEG LVILDDGSKD
HILSQKMACP NGHDIGFTEL SPRMFSFNSP YGACETCDGL GSLLEFDEDL LVNDPELSLV
DGCIEAWAGS KSNGFWFMAT LKSLSDSLKF KMNTPWKDLP EKTRQTILYG DKKIKIEYDF
RGANSHYEFT KEYEGVIPNL QRRYKETKSD SMRQWFESYM TNHPCPSCKG KRLKRESLSV
KVHNVPVDEF TSYSIEKALN FVQNLKVTGA EEIIAKPILK EIHQRLSFLN DVGVGYLTLE
RSAGSLSGGE AQRIRLATQI GSRLMGVLYI LDEPSIGLHQ RDNTKLVSTL KNLRDLGNTV
LVVEHDQETM EESDWLIDMG PGAGVHGGSI VCAGTPAEVS KHKNSLTGKY LSGRLKVPIP
AKLREGNGSK LQIIGAKENN LKNIDVNIPL GKLVVITGVS GSGKSTLIND ILYNAAAHKV
MKMKTLAGKH KTIKGFENID KIINIDQSPI GRTPRSNPAT YTGLFTPIRE MFAGLEEAKL
RGYGPGRFSF NVSGGRCETC EGDGILKIEM HFLPDVYVTC EVCKGKRYNQ ETLEVRYKGK
NIFDVLEMTV EDANQFFENI PIVKRKLETL LEVGLGYIRL GQPATTFSGG EAQRIKLATE
LSKRPTGKTL YILDEPTTGL HFEDVRRLSE VLHTLVDRGN SMIVIEHNLD VIKQADWIVD
MGPEGGDGGG LVIAEGIPKD IAKIKNSYTG QYLKKIFTSS EKISRKTK