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Database: UniProt
Entry: A0A1H3A6X1_9RHOB
LinkDB: A0A1H3A6X1_9RHOB
Original site: A0A1H3A6X1_9RHOB 
ID   A0A1H3A6X1_9RHOB        Unreviewed;       954 AA.
AC   A0A1H3A6X1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN04488238_106232 {ECO:0000313|EMBL:SDX25457.1};
OS   Roseicitreum antarcticum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Roseicitreum.
OX   NCBI_TaxID=564137 {ECO:0000313|EMBL:SDX25457.1, ECO:0000313|Proteomes:UP000198539};
RN   [1] {ECO:0000313|EMBL:SDX25457.1, ECO:0000313|Proteomes:UP000198539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8894 {ECO:0000313|EMBL:SDX25457.1,
RC   ECO:0000313|Proteomes:UP000198539};
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; FNOM01000006; SDX25457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3A6X1; -.
DR   STRING; 564137.SAMN04488238_106232; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000198539; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198539};
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..937
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   954 AA;  105291 MW;  58EC0A7B5060F577 CRC64;
     MAEQKFIEVR GAREHNLKNI DVDIPRDQLV VITGLSGSGK SSLAFDTIYA EGQRRYVESL
     SAYARQFLDM MQKPDVDHIS GLSPAISIEQ KTTSKNPRST VGTVTEIYDY MRLLFARAGT
     PFSPATGKPI EAQQVQDMVD RVMGLDEGTR AYLLAPIIRD RKGEYRKEFL ELRKQGFQRV
     KVDGQFYELD EPPTLDKKFR HDIDVVVDRL VVRTGLETRL ADSLRTALDL ADGIAVLEMA
     DAGEDGVAER ITFSEKFACP VSGFTIPEIE PRLFSFNAPF GACPDCDGLG LELFFDERLV
     VPDGALTLAN GAIAPWRKGK TPYFLQTIQS LAAHYEFNPK TLWKDLPPHV HQVLLYGSNG
     EELPFRYDEG GRIYNVTRAF EGVIPNMERR YRETDSNWVR EDFEQYQNNR DCATCGGHRL
     RAEALAVKIG GLHVGEVVDK SIREVYDWVQ SVPDHLTNQK NEIARAILKE IRERVGFLVN
     VGLDYLTLSR RAGTLSGGES QRIRLASQIG SGLTGVLYVL DEPSIGLHQR DNDRLLTTLK
     NLRDQGNTVI VVEHDEEAIR EADYVFDIGP GAGVHGGRVV SHGTPAQVMA DAGSVTGQYL
     SGARQIAVPS VRRKGNGKKI KVVKATGNNL RDMSAEFPLG KFVCVTGVSG GGKSTLTIET
     LFKTASMRLN GARQTPAPCE TIKGLEHLDK VIDIDQRPIG RTPRSNPATY TGAFGPIRDW
     FAGLPESKTR GYKPGRFSFN VKGGRCEACQ GDGVLKIEMN FLPDVYVTCE TCKGARYNRE
     TLEVLFKGKS IADVLEMTVE EAQGFFQAVP SIREKMDALM RVGLGYIKVG QQATTLSGGE
     AQRVKLSKEL ARRSTGRTLY ILDEPTTGLH FEDVRKLLEV LHELVEQGNT VVVIEHNLDV
     VKTADWVIDI GPEGGDGGGQ IVAVGTPEAV AAVEGSHTGH YLKSLLDPRK FAAE
//
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