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Database: UniProt
Entry: F8GKP2_NITSI
LinkDB: F8GKP2_NITSI
Original site: F8GKP2_NITSI 
ID   F8GKP2_NITSI            Unreviewed;       939 AA.
AC   F8GKP2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316, ECO:0000256|HAMAP-Rule:MF_00205};
DE            Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156, ECO:0000256|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN   OrderedLocusNames=Nit79A3_3174 {ECO:0000313|EMBL:AEJ02909.1};
OS   Nitrosomonas sp. (strain Is79A3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ02909.1};
RN   [1] {ECO:0000313|EMBL:AEJ02909.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ02909.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA   Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT   "Complete sequence of Nitrosomonas sp. Is79A3.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_00205}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000256|ARBA:ARBA00038000, ECO:0000256|HAMAP-Rule:MF_00205}.
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DR   EMBL; CP002876; AEJ02909.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8GKP2; -.
DR   STRING; 261292.Nit79A3_3174; -.
DR   KEGG; nii:Nit79A3_3174; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_4; -.
DR   OrthoDB; 9809851at2; -.
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   CDD; cd03270; ABC_UvrA_I; 1.
DR   CDD; cd03271; ABC_UvrA_II; 1.
DR   Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR   Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00630; uvra; 1.
DR   PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1.
DR   PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00205};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00205}.
FT   DOMAIN          605..934
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         251..278
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         737..763
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         638..645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   939 AA;  104019 MW;  A7AAEAB01FB75D1D CRC64;
     MESIKIRGAR THNLKNISLD LPRNKLVVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLQLMEK PDVDLIEGLS PAIAIEQKAT SHNPRSTVGT VTEIHDYLRL LFARVGDPHC
     PEHNIILTAQ SVSQMVDHVL QLPLDTRLMI LSPLIVERKG EQAELFDELR AQGFVRLRID
     GEVYEIDALP KLQKNQKHTI EVVIDRLKVS PDAKQRLAES FEVALRHSEG RALAVEMDTG
     AEHLFSAKFS CPVCSYSLSE LEPRLFSFNN PLGACNKCDG LGQITFFDPA RVVAFPHLSL
     AAGAVKNWDR RNQFYFQLLT ALSKHYEFDL ETPFENLDEP IRNIILHGSG KEKIHFSYLT
     EGGRKHQETH AFEGIIPNLT RRYKETESQT VREELAKYLN AQTCPECHGT RLCQAARHVH
     VAGQAIYEIS AFPLKKAKLF FDQIELTGHK HAIAERIVKE ISSRVQFLNN VGLDYLSLDR
     SADTLSGGES QRIRLASQIG SGLTGVMYVL DEPSIGLHQR DNGRLLDTLK NLRDLGNSVI
     VVEHDQDAIQ IADYVVDMGP GAGEHGGFVV AQGNPQAIQE NNDSLTGKYL SGKLSIPIPE
     KRHAPNPERV LRIDGASGNN LKNVTLNLPV GLFVCVTGVS GSGKSTLINE TLHRAVARHL
     YASNAEPAPY QQIDGLAFFD KVINMDQSPI GRTPRSNPAT YTGLFTPIRE LFAGVPQARE
     RGYAPGRFSF NVKGGRCEAC QGDGVIKVEM HFLPDIYVTC DVCHGRRYNR ETLEIQYKGK
     NINEILQMTV EKAAEFFTPV PVVARKLQTL LEVGLGYITL GQSATTLSGG EAQRVKLSLE
     LSKRDTGRTL YILDEPTTGL HFQDIDLLLK VLHRLRDHGN TVVVIEHNLD VIKTADWIID
     LGPEGGDGGG CIIAEGTPEA IAVNTNSFTG HYLQSMLTK
//
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