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Database: UniProt
Entry: A0A239H2X1_9RHOB
LinkDB: A0A239H2X1_9RHOB
Original site: A0A239H2X1_9RHOB 
ID   A0A239H2X1_9RHOB        Unreviewed;       955 AA.
AC   A0A239H2X1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN05421757_103217 {ECO:0000313|EMBL:SNS75531.1};
OS   Tropicimonas sediminicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tropicimonas.
OX   NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNS75531.1, ECO:0000313|Proteomes:UP000198426};
RN   [1] {ECO:0000313|EMBL:SNS75531.1, ECO:0000313|Proteomes:UP000198426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29339 {ECO:0000313|EMBL:SNS75531.1,
RC   ECO:0000313|Proteomes:UP000198426};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZOY01000003; SNS75531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239H2X1; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000198426; 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; 3.30.190.20; -; 1.
DR   Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR   Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
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:UP000198426};
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          611..943
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         746..772
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         647..654
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   955 AA;  105965 MW;  C76010E5EC582755 CRC64;
     MPEQKFIEVR GAREHNLKNI DVDIPRDELV VITGLSGSGK SSLAFDTIYA EGQRRYVESL
     SAYARQFLDM MEKPDVDHIT GLSPAISIEQ KTTSKNPRST VGTVTEIYDY LRLLFARVGT
     PYSPATGLPI EAQQVQDMVD RVMAMEEGTR AYLLAPIVRD RKGEYRKEFL ELRKQGFQRV
     KVDGAFHDLD DAPKLDKKFR HDIDVVVDRI VVREGMETRL ADSFRTALDL ASGIAILETA
     PREEEGEPER ITFSENFACP VSGFTIPEIE PRLFSFNAPF GACPHCDGLG VELFFDERLV
     VPDVTLKIYD GALAPWRKGK SPYFLQTIEA IAKHYEFDKN ARWKDLPKKV QQVFLHGSGD
     EEIEFRYDEG GRVYQVTRSF EGVIPNMERR YRETDSAWIR EEFERYQNNR PCGSCGGYRL
     RPEALAVKIA GLHVGQVVQM SIREAFDWVD AVPEKLTSQK NEIARAILKE IRERLGFLNN
     VGLEYLTLSR NAGTLSGGES QRIRLASQIG SGLTGVLYVL DEPSIGLHQR DNDRLLGTLK
     NLRDQGNTVI VVEHDEEAIR EADYVFDIGP GAGVHGGQVV AKGTPGEIAA NPDSITGDYL
     SGKREIPVSQ LRREGNGKKL TVVKATGNNL KEVTADFPLG KFVCVTGVSG GGKSTLTIET
     LFKTASMRLN GARQTPAPCE TIKGLEHLDK VIDIDQRPIG RTPRSNPATY TGAFTPIRDW
     FAGLPEAKAR GYKPGRFSFN VKGGRCEACQ GDGVIKIEMH FLPDVYVTCE TCHGARYNRE
     TLEIKFKGKS IADVLDMTVE DAQEFFKAVP SIREKMDALV RVGLGYIKVG QQATTLSGGE
     AQRVKLSKEL AKRSTGRTLY ILDEPTTGLH FEDVRKLLEV LHELVEQGNT VVVIEHNLDV
     IKTADWIIDI GPEGGDGGGT VVATGTPEEV AEVAGSHTGR YLKPMLDAAR RHAAE
//
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