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Entry: A0A1I6RE43_9PSEU
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ID   A0A1I6RE43_9PSEU        Unreviewed;       989 AA.
AC   A0A1I6RE43;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05660874_02130 {ECO:0000313|EMBL:SFS63011.1};
OS   Saccharopolyspora flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=95161 {ECO:0000313|EMBL:SFS63011.1, ECO:0000313|Proteomes:UP000198852};
RN   [1] {ECO:0000313|EMBL:SFS63011.1, ECO:0000313|Proteomes:UP000198852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44771 {ECO:0000313|EMBL:SFS63011.1,
RC   ECO:0000313|Proteomes:UP000198852};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00205}.
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DR   EMBL; FOZX01000003; SFS63011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6RE43; -.
DR   STRING; 95161.SAMN05660874_02130; -.
DR   Proteomes; UP000198852; 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; 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          657..985
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         788..814
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         689..696
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   989 AA;  108551 MW;  8D74E6D2DEE558C2 CRC64;
     MDVATSRPDA APAVPLPAAG GRSQPARSRN TRTFSEGITV ADRLVVRGAR EHNLRGIDLD
     LPRDSLIVFT GLSGSGKSSL AFDTIFAEGQ RRYVESLSAY ARQFLGQMDK PDVDFIEGLS
     PAVSIDQKST SRNPRSTVGT ITEVYDYLRL LYARAGKPHC PTCGEAISKQ TPQQIVDQVL
     EMPERAKFQV LAPVVRGRKG EYVDLFEQLR SSGYARARVD GVVHSLDDPP KLKKQEKHDI
     AVVVDRLTVK SGAKQRLTDS VETALRLADG LVLVEFIDLE ESDPGRERKF SENLACPNGH
     PLGVDELEPR SFSFNSPYGA CPECAGLGIR KEVDPELVVP DEDLSLGDGA IAPWAGGHTA
     EYFTRLLTSL SEAIGFRMDT PWRQLPTKVK KAVLHGTDDQ VHVRYRNRYG RTRSYYASYE
     GVIPFLERRL EQTESDYARE KYEGYMRDVP CPACDGTRLK PEILAVTMEN EDDELSIAEV
     SALSVRECAE FLNALVLGPR EQMIAGAVLK EIQARLGFLL DVGLDYLSLD RAAGTLSGGE
     AQRIRLATQI GSGLVGVLYV LDEPSIGLHQ RDNHRLLETL SRLRDLGNTL IVVEHDEDTV
     RAADWVVDIG PGAGEHGGEV VHSGPYKELL KNKQSLTGAY LARRKEIPVP TERRVPDRKR
     QLTVVGAREH NLRKIDVSFP LGLLTAVTGV SGSGKSTLVN DILASVLANK LNGARQVPGR
     HTRVKGLEHV DKLVQVDQSP IGRTPRSNPA TYTGVFDHIR KLFAATTEAK VRGYQPGRFS
     FNIKGGRCEA CAGDGTLKIE MNFLPDVYVP CEVCKGARYN RETLEVHYKG KTIAEVLDMP
     IEEAAEFFEP INAIHRHLKT LVDVGLGYVR LGQPAPTLSG GEAQRVKLAS ELQKRSTGKT
     VYILDEPTTG LHFEDIRKLL GVINGLVDKG NTVIVIEHNL DVIKTADWIL DLGPEGGNGG
     GLLLAEGMPE DIAEVEESHT GRFLAEVLD
//
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