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Database: UniProt
Entry: A0A1E1F6R7_9SPHN
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ID   A0A1E1F6R7_9SPHN        Unreviewed;       971 AA.
AC   A0A1E1F6R7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=SCLO_1031640 {ECO:0000313|EMBL:BAV66204.1};
OS   Sphingobium cloacae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=120107 {ECO:0000313|EMBL:BAV66204.1, ECO:0000313|Proteomes:UP000218272};
RN   [1] {ECO:0000313|EMBL:BAV66204.1, ECO:0000313|Proteomes:UP000218272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10874 {ECO:0000313|EMBL:BAV66204.1,
RC   ECO:0000313|Proteomes:UP000218272};
RA   Ootsuka M., Nishizawa T., Ohta H.;
RT   "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT   Sphingobium cloacae JCM 10874T.";
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; AP017655; BAV66204.1; -; Genomic_DNA.
DR   RefSeq; WP_066514674.1; NZ_AP017655.1.
DR   AlphaFoldDB; A0A1E1F6R7; -.
DR   KEGG; sclo:SCLO_1031640; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000218272; 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; 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:UP000218272};
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          339..618
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          620..960
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         763..789
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         664..671
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   971 AA;  105804 MW;  6BB9B0BE97DC7703 CRC64;
     MSLTHISVRG AREHNLKGVD VDLPRDALVV ITGLSGSGKS SLAFDTIYAE GQRRYVESLS
     AYARQFLEMM QKPDVEHIEG LSPAISIEQK TTSRNPRSTV ATVTEIYDYM RLLWARVGIP
     YSPATGLPIA AQTVSQMVDR VMQLPEGTRF YLLAPVVRGR KGEYRKELAE WQKAGFTRVR
     IDGELYAIEE APALDKKYKH DIEVVVDRLA VAPDMSTRLA DSFETALKLA DGLAYVDLAD
     GIVPGREDET QSSGKMKNSG IPANRIVFSE KFACPVSGFT IPEIEPRLFS FNAPQGACPA
     CDGLGERQEF DPELVVPNEA LSLKKGAVVP WAKSNPPSPY YMQVLGSLAK EFGFSLDTPW
     QDLPGEVKLI ILHGTGGKPV TLRFQDGKKS YEVRKPFEGV IGNLNRRLLQ TESAWMREEL
     SKYQTAMPCE TCDGARLKPE ALAVKIAGED ISLSTRRSVV DALAFFSTLP EKLNDQQNQI
     AKAILKEIVE RLGFLNNVGL DYLNLDRTSG TLSGGESQRI RLASQIGSGL SGVLYVLDEP
     SIGLHQRDND RLLITLKRLR DLGNTVIVVE HDEDAIRAAD YIVDMGPGAG VHGGSIVAQG
     SLNQLLAHKD SLTADYLNGT RRIDVPAKRR KGTGKKLTVH NARANNLRGV TASIPLGTFT
     CITGVSGSGK SSFTIDTLYA ASARALNGAR IVAGAHDKVT GLENCDKVID IDQSPIGRTP
     RSNPATYTGA FTNIRDWFAG LPEAQARGYK PGRFSFNVKG GRCEACQGDG VLKIEMHFLP
     DVYVTCDVCH GARYNRETLE VKFKGKSIAD VLDMTVEDAV EFFKAVPPIR DKMAMLAEVG
     LGYVKVGQQA TTLSGGEAQR VKLAKELSRR ATGNTLYILD EPTTGLHFED VRKLLEVLHA
     LVEQGNSVVV IEHNLDVIKT ADWIIDMGPE GGVKGGEVVA EGTPEKVAKN ARSFTGRYLA
     PLLGMEAVAA E
//
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