UVRA_CLOPE
ID UVRA_CLOPE Reviewed; 939 AA.
AC Q8XNI5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=CPE0348;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB80054.1; -; Genomic_DNA.
DR RefSeq; WP_011009759.1; NC_003366.1.
DR AlphaFoldDB; Q8XNI5; -.
DR SMR; Q8XNI5; -.
DR STRING; 195102.gene:10489604; -.
DR PRIDE; Q8XNI5; -.
DR EnsemblBacteria; BAB80054; BAB80054; BAB80054.
DR KEGG; cpe:CPE0348; -.
DR HOGENOM; CLU_001370_0_2_9; -.
DR OMA; PFEGIIP; -.
DR Proteomes; UP000000818; 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; 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; 1.
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..939
FT /note="UvrABC system protein A"
FT /id="PRO_0000093046"
FT DOMAIN 309..588
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 608..936
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 252..279
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 739..765
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 32..39
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 939 AA; 104727 MW; CC8D547AF186987C CRC64;
MKDKIIVKGA KVHNLKNVSL EIPRDKLIVF TGLSGSGKSS LAFDTIYAEG QRRYVESLSS
YARQFLGQMD KPDVESIEGL SPAISIDQKT TSRNPRSTVG TVTEIYDYLR LLYARVGVPH
CPKCGKEITQ QSVDQIVDQI MELPERSKIM ILAPIIRGRK GTHEKVLENI KKQGFVRARI
DGEIYDLTED EIKLEKNIKH NIEAVVDRII VKDGIEGRLT DSIETSLKMA EGLVLVNIIG
EEDRLYSEHF ACADCGISID ELAPRMFSFN SPFGKCERCD GLGTLMEIDE DLVVPNKDLS
IRGGAISTWG DSRMKEESWT YCVLKALMEK YNFDLDTPYK DLPKKVQEVL MYGEPEKLKV
TYTKENVTAV YNHSFEGEIN NLRRRYMETN SDTMKAEIEK YMSDNPCPKC KGARLKPEAL
AVTVGGKNIF EFTSMAIREE LDFINSINFS EKDKIISSQI IKEIQSRLSF LINVGLDYLD
LARKAGTLSG GEAQRIRLAT QIGSQLMGVL YILDEPSIGL HQRDNDRLIS TLKQLRDVGN
TLIVVEHDED TMREADYIVD IGPGAGEHGG KIVASGTLDE IMSNENSLTG KYLTGAKKVE
LPEERRKGNG NFITVKGAKE NNLKNVTAKF PLGTLTMVTG VSGSGKSTLV NEILYKGLNK
IVNKAKDLPG KFKEITGYEN IDKIIDIDQS PIGRTPRSNP ATYTGTFDII RELFSQTQEA
KMRGYKPGRF SFNVKGGRCE ACSGDGIIKI EMQFLSDVYV PCEVCKGKRY NRETLEVKYK
GKNIADVLNM TVEEALEFFE NIPRIKNKLQ TLMDVGLGYI RLGQPSTQLS GGEAQRIKLA
YELSKRSTGK TLYILDEPTT GLHIHDVNRL VKILQRLVDG GNTVIVIEHN LDMIKCADYI
VDLGPEGGDK GGTIIATGTP EKIAGAKESY TGKYLKKYL
