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Database: UniProt
Entry: A0A2K8L283_9PROT
LinkDB: A0A2K8L283_9PROT
Original site: A0A2K8L283_9PROT 
ID   A0A2K8L283_9PROT        Unreviewed;       936 AA.
AC   A0A2K8L283;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ORFNames=Ga0123462_0569 {ECO:0000313|EMBL:ATX81440.1};
OS   Mariprofundus ferrinatatus.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=1921087 {ECO:0000313|EMBL:ATX81440.1, ECO:0000313|Proteomes:UP000231637};
RN   [1] {ECO:0000313|EMBL:ATX81440.1, ECO:0000313|Proteomes:UP000231637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP-8 {ECO:0000313|EMBL:ATX81440.1,
RC   ECO:0000313|Proteomes:UP000231637};
RA   McAllister S.M., Kato S., Chan C.S., Chiu B.K., Field E.K.;
RT   "Isolation and genomic insights into novel planktonic Zetaproteobacteria
RT   from stratified waters of the Chesapeake Bay.";
RL   Submitted (DEC-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; CP018800; ATX81440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8L283; -.
DR   KEGG; mfn:Ga0123462_0569; -.
DR   OrthoDB; 5287123at2; -.
DR   Proteomes; UP000231637; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000231637};
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          601..933
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         736..762
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         637..644
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   936 AA;  102781 MW;  5E075EF0961F9FCC CRC64;
     MSKPVIRVEG ARVHNLKNIS LEMPRDKLVV ITGVSGSGKS SLAFDTLYAE GQRRYVESLS
     AYARQFLGMM ERPDVDAIEG LSPAISIEQK TTSRNPRSTV GTITEVYDYL RLLFARIGQP
     YCHGCGKPIT SQPASVIIDQ LEKLEEGTKL QLLAPIARGK KGEFRKELEK AGKDGFVRVR
     IDGEVMPLED APQLEKNIKH NIELVVDRLV MRDGIRTRLA DSVETALRYG EGMMIALIGA
     EEQLFSERFA CPDCNISYPD IEPRLFSFNS PVGACPACDG LGSKTVFDPD LVVPDAGLSV
     AAGAIEPWAG RETFMYRQTL EAVAAHADVS MDMPFGELPE SARNAFLYGS GREKIRFVYE
     TPGQNRVIER PFEGVIPNLE RRWRESSSDD VREALEKYIN TIDCPGCNGS RLTKAARHVR
     INDVSLPEVV AMPLREAVAW VKGLKLSDQQ QAIADKVVEE ISARLGFMIE VGLDYLSLER
     TSGTLSGGEA QRIRLATQIG SALVGVLYIL DEPSIGLHQR DNDRLLATLR RLRDLGNSVL
     VVEHDEDAIR SADWIIDMGP LAGEHGGEVV AQGTLKDILK SKTLTSDYLS GRKKIVVPKR
     RKVPSKHPVI GVEGACEHNL QQVTAEFPVS RFSCVTGVSG SGKSTLTNDT LFRGFARAKG
     LKSERVGAHG RLIGSDLVDK IIDIDQSPIG RTPRSNPATY TGLFTPIREL FAQVPESRAR
     GYKPGRFSFN VKGGRCEACQ GDGIIKVEMH FLPDVYVHCE SCQGKRYNRE TLDIRYKGKT
     IDEVLHMTVE EALEFFAAIP PLKNRLMTLS QVGLGYIQLG QSATTLSGGE AQRVKLSREL
     ARRATGDTLY ILDEPTTGLH FHDVAKLLDV LHALVDRGNT VIVIEHNLDV IKTADWIVDM
     GPEGGDRGGT VVVAGTPEQV AACKASHTGH YLKGCL
//
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