UVRA_BACSU
ID UVRA_BACSU Reviewed; 957 AA.
AC O34863;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
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=BSU35160;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(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; AF017113; AAC67271.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15533.1; -; Genomic_DNA.
DR PIR; F69729; F69729.
DR RefSeq; NP_391396.1; NC_000964.3.
DR RefSeq; WP_003228057.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34863; -.
DR SMR; O34863; -.
DR IntAct; O34863; 1.
DR MINT; O34863; -.
DR STRING; 224308.BSU35160; -.
DR PaxDb; O34863; -.
DR PRIDE; O34863; -.
DR EnsemblBacteria; CAB15533; CAB15533; BSU_35160.
DR GeneID; 936646; -.
DR KEGG; bsu:BSU35160; -.
DR PATRIC; fig|224308.179.peg.3806; -.
DR eggNOG; COG0178; Bacteria.
DR InParanoid; O34863; -.
DR OMA; PFEGIIP; -.
DR PhylomeDB; O34863; -.
DR BioCyc; BSUB:BSU35160-MON; -.
DR Proteomes; UP000001570; 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; 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..957
FT /note="UvrABC system protein A"
FT /id="PRO_0000093035"
FT DOMAIN 309..587
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 607..935
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 738..764
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 639..646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 957 AA; 106032 MW; 8DE6CD209F3A40A6 CRC64;
MAMDRIEVKG ARAHNLKNID VTIPRDQLVV VTGLSGSGKS SLAFDTIYAE GQRRYVESLS
AYARQFLGQM DKPDVDAIEG LSPAISIDQK TTSRNPRSTV GTVTEIYDYL RLLYARVGKP
HCPEHGIEIT SQTIEQMVDR ILEYPERTKL QVLAPIVSGR KGAHVKVLEQ IRKQGYVRVR
IDGEMAELSD DIELEKNKKH SIEVVIDRIV VKEGVAARLS DSLETALRLG EGRVMIDVIG
EEELMFSEHH ACPHCGFSIG ELEPRLFSFN SPFGACPTCD GLGMKLEVDA DLVIPNQDLS
LKENAVAPWT PISSQYYPQL LEAVCTHYGI DMDVPVKDLP KHQLDKVLYG SGDDLIYFRY
ENDFGQIREG EIQFEGVLRN IERRYKETGS DFIREQMEQY MSQKSCPTCK GYRLKKEALA
VLIDGRHIGK ITELSVADAL AFFKDLTLSE KDMQIANLIL REIVERLSFL DKVGLDYLTL
SRAAGTLSGG EAQRIRLATQ IGSRLSGVLY ILDEPSIGLH QRDNDRLISA LKNMRDLGNT
LIVVEHDEDT MMAADYLIDI GPGAGIHGGQ VISAGTPEEV MEDPNSLTGS YLSGKKFIPL
PPERRKPDGR YIEIKGASEN NLKKVNAKFP LGTFTAVTGV SGSGKSTLVN EILHKALAQK
LHKAKAKPGS HKEIKGLDHL DKVIDIDQAP IGRTPRSNPA TYTGVFDDIR DVFAQTNEAK
VRGYKKGRFS FNVKGGRCEA CRGDGIIKIE MHFLPDVYVP CEVCHGKRYN RETLEVTYKG
KSISDVLDMT VEDALSFFEN IPKIKRKLQT LYDVGLGYIT LGQPATTLSG GEAQRVKLAS
ELHKRSTGRT LYILDEPTTG LHVDDIARLL VVLQRLVDNG DTVLVIEHNL DIIKTADYIV
DLGPEGGAGG GTIVASGTPE EITEVEESYT GRYLKPVIER DKTRMKSLLK AKETATS
