UVRA_METTH
ID UVRA_METTH Reviewed; 962 AA.
AC O26543;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=MTH_443;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB84949.1; -; Genomic_DNA.
DR PIR; H69157; H69157.
DR AlphaFoldDB; O26543; -.
DR SMR; O26543; -.
DR STRING; 187420.MTH_443; -.
DR PRIDE; O26543; -.
DR EnsemblBacteria; AAB84949; AAB84949; MTH_443.
DR KEGG; mth:MTH_443; -.
DR PATRIC; fig|187420.15.peg.413; -.
DR HOGENOM; CLU_001370_0_2_2; -.
DR OMA; PFEGIIP; -.
DR Proteomes; UP000005223; 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; 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; PF00005; ABC_tran; 1.
DR Pfam; PF17755; UvrA_DNA-bind; 1.
DR Pfam; PF17760; UvrA_inter; 1.
DR SMART; SM00382; AAA; 2.
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; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..962
FT /note="UvrABC system protein A"
FT /id="PRO_0000093122"
FT DOMAIN 319..597
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 617..944
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 748..774
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 649..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 962 AA; 108396 MW; 2C0EF7FC41CCD060 CRC64;
METLRIMSGK IVIKGAREHN LQNVDLELPR DKFIVITGIS GSGKSSLAFD TIYAEGQRRY
VESLSAYARQ FLGQMKKPEM DYIEGLSPAI SIDQKTTRVN PRSTVGTITE IYDYLRLLFA
RIGKPHCYLC GREIEQQTST QIVDRIMDDG EGERIIILAP VVRDRKGEHQ RVFERLREQG
FVRVRVDGEI HDLEDEFDLD RNRKHSIDVV VDRLVVRRDT EFRKRLADSV ETALQLGEGT
VRVPSTMTPG EERIYSEHFA CPGTAGINFE EISPRMFSFN SPHGACPECN GLGSKLEIDP
DLVVPYPERS INEGAIVPWS KSGKRDNYYH QMLRAVAEHY GFSLDTPFRD LDEEHRRAIL
YGTDEKIQFV FQRKNRTYRV NRRFEGVIPR MERIYMETKS NYMRTYIGRF MSNHACPVCG
GSRLRPESLS VTINGRSIHD VVEMSIREAH EFFDSLKLTE REEYIAREVL KEIRERLRFL
IDVGLDYLTL SRSSGTLSGG EAQRIRLATQ IGSGLVGVLY ILDEPSIGLH QRDNRRLIET
LKRLRDLGNT LIVVEHDEET ILSADHVVDI GPGAGEHGGC VVAEGTPEEI MEDPDSLTGA
YLSGRETIPL PEVRRRPSGR YLTVRGAAEN NLREIDVRIP LGLFTCVTGV SGSGKSTLVN
DILYRGVYER LNHKHMNAGR HTDIEGLQHI DKVVMIDQSP IGRTPRSNPA TYTGVFTHIR
ELFAQTPEAR KRGYRPGRFS FNVKGGRCEA CGGDGIIKIE MHFLADVYVP CEVCRGRRYN
EETLEIRYRG RNIAEVLDMT VEEALEFFEN IPQVRRKLQT LYDVGLGYIK LGQPATTLSG
GEAQRVKLAK ELSRRSTGST LYILDEPTTG LHFDDIKKLL NVLGRLVDAG NTAVVIEHNL
DVIKSADHII DLGPEGGERG GLVVAEGTPE EVAASGTHTG RFLREVLADE RSQKVPVGQD
TG
