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Entry: A0A1A8TBI1_9GAMM
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ID   A0A1A8TBI1_9GAMM        Unreviewed;       939 AA.
AC   A0A1A8TBI1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ECO:0000313|EMBL:SBS29475.1};
GN   ORFNames=MAQ5080_01404 {ECO:0000313|EMBL:SBS29475.1};
OS   Marinomonas aquimarina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=295068 {ECO:0000313|EMBL:SBS29475.1, ECO:0000313|Proteomes:UP000092627};
RN   [1] {ECO:0000313|EMBL:SBS29475.1, ECO:0000313|Proteomes:UP000092627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5080 {ECO:0000313|EMBL:SBS29475.1,
RC   ECO:0000313|Proteomes:UP000092627};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; FLOC01000006; SBS29475.1; -; Genomic_DNA.
DR   RefSeq; WP_067207616.1; NZ_LTAV01000007.1.
DR   AlphaFoldDB; A0A1A8TBI1; -.
DR   STRING; 295068.MAQ5080_01404; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000092627; Unassembled WGS sequence.
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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000092627};
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          309..592
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          607..936
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         739..765
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         639..646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   939 AA;  103516 MW;  1C357AF1BD7FC9F1 CRC64;
     MDTITLRGAR THNLKNIDLD IPRDKLVVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSTY
     ARQFLSMMEK PDIDHIEGLS PAISIEQKST SHNPRSTVGT ITEVYDYLRL LFARAGQPRC
     PDHGEPLEAQ TISQMVDKVL ALPEESKMMM LAPIIKDRKG EHLHTISELL SKGFVRARID
     GIVVDLDDAP ALEKNKKHTI EVVIDRFKVR PDLQLRLAES FETCLSLSDG IAKVINMDDE
     NDELVFSSKF ACPVCGYAIT ELEPRLFSFN NPNGACQTCD GLGTQQAFDA DRVIQDESLT
     LGEGAIRGWG RRSIFYFQQL NALANFYGFD INSKFKDIPV AYQDIILNGS GKDKIDFVYI
     NERGDKMTRS HAFEGVLPNL NRRYHETESD SVRDDLSQYI STKPCSSCHG TRLNKAARNV
     FIADETLPDI VKKPIAECLQ YFETLQLQGA KAEIAEKILK EIRDRLSFLV NVGLDYLTLD
     RKADSLSGGE AQRIRLASQI GAGLVGVMYI LDEPSIGLHQ RDNERLIGTL TRLRDLGNTV
     IVVEHDEDAI RVADHLIDIG PGAGVHGGQV IASGTPQDIM DCEASITGQY LTGKRKIEIP
     ALRHQATQGK QITLHGAQGN NLNDVTLNIP VGVMTCVTGV SGSGKSTLIN GTLYPLAATA
     LNGATTLTAA EHSHIEGLDH FDKCVDIDQS PIGRTPRSNP ATYTGIFTPM RELFAATQEA
     RSRGYKPGRF SFNVKGGRCE ACQGDGVIKV EMHFLPDVYV PCDVCKGHRY NRETLEITYK
     GKNIHECLEM TIEEAREFFD PVPSIARKLQ TLIDVGLGYI RLGQAATTLS GGEAQRVKLA
     KELSKRDTGK TLYILDEPTT GLHFADIELL LSVLHRLRDH GNTIVVIEHN LDVIKTADWI
     VDLGPEGGSG GGYIVAEGTP ETVAEHETSH TARFLKPML
//
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