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UVRA_MALP2
ID   UVRA_MALP2              Reviewed;         952 AA.
AC   Q8EUL1;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=MYPE9100;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(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; BA000026; BAC44701.1; -; Genomic_DNA.
DR   RefSeq; WP_011077730.1; NC_004432.1.
DR   AlphaFoldDB; Q8EUL1; -.
DR   SMR; Q8EUL1; -.
DR   STRING; 272633.26454373; -.
DR   EnsemblBacteria; BAC44701; BAC44701; BAC44701.
DR   KEGG; mpe:MYPE9100; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_14; -.
DR   OMA; PFEGIIP; -.
DR   OrthoDB; 152379at2; -.
DR   Proteomes; UP000002522; 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; 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..952
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093065"
FT   DOMAIN          315..596
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          616..945
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         258..285
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         747..773
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         648..655
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   952 AA;  106312 MW;  745C0F3996D3DC2E CRC64;
     MNNKVNTRDF IVVKGARENN LKNVDIDIPK NKFVVMTGLS GSGKSSLAFD TIYAEGQRRY
     LESLSSYARQ FLGGNEKPDV DSIEGLSPAI SIDQKTTSHN PRSTVGTVTE IYDYLRLLFS
     RIGKPYCPNG HGLISTLSIK QMIDTVYENK EESKIQILSP IISQEKGTFK NKIEELKRQG
     YLRLRIDGNI YSLDDEIELE KTKKHNIDIL IDRIILNNDT VTRSRIYDAI EKSVKEANGK
     VIVLVDDKEL FFSQNHACNE CGFSIPELEP RFFSFNSPVG ACKSCNGIGF NFLPDTAKIV
     PDPSLSIKEG AIAYFRSVMM TPTMDLKREM SVWKEHDINL DVPFKELSKK EKNIIFYGDE
     DIGELKIDVN EQSIYSSSSF LYNNGLVNLI MRRFSETQSE RAREYYEKFM SNLSCPSCNG
     QKLSIEALSV KINNKNIIDL TEKNINDLTN FFIELELNET DRNIAHLALK EIVDRLSFLE
     NVGLNYLTLS RSASTLSGGE SQRIRLATQI GSSLTGVLYV LDEPSIGLHQ KDNEKLIETL
     KKMRDLGNTL IVVEHDEDTI RASDYLIDIG PKAGDFGGEV VAAGTVSEVS ENKKSITAQY
     LSGKLKIEVP SKRRHGNGKT IELVGASGNN LKNVTVSFPL NKLIAVTGVS GSGKSTLINE
     TLIKGIEKKL TNPFIVPAPF KDIKGLKNVD KIIKVSQDPI GRTPRSNPAT YVSVFDDIRD
     LFANTKEAKA RGFQKGRFSF NVSGGRCENC SGDGLIKIEM HFLPDVFVKC ESCNGKKYNQ
     ETLQVLYKGK SIYDVLEMSV VEARDFFYEI PEIKRKLDLM VEVGIDYLKL GTSSTHLSGG
     EAQRIKLAKY LQKRATGKTI YVLDEPTTGL HIHDIAKLIT VLNRIVDNGD TVIVVEHNLD
     LIKCADYVID LGPDGGINGG QLVAYGTPEE IIEKKAVSYT GLFLEKNMYK DK
 
 
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