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Entry: A0A0K2JEQ9_SPIKU
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ID   A0A0K2JEQ9_SPIKU        Unreviewed;       950 AA.
AC   A0A0K2JEQ9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ECO:0000313|EMBL:ALA97075.1};
GN   ORFNames=SKUN_00151 {ECO:0000313|EMBL:ALA97075.1};
OS   Spiroplasma kunkelii CR2-3x.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=273035 {ECO:0000313|EMBL:ALA97075.1, ECO:0000313|Proteomes:UP000062963};
RN   [1] {ECO:0000313|EMBL:ALA97075.1, ECO:0000313|Proteomes:UP000062963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR2-3x {ECO:0000313|EMBL:ALA97075.1,
RC   ECO:0000313|Proteomes:UP000062963};
RX   PubMed=26494665;
RA   Davis R.E., Shao J., Dally E.L., Zhao Y., Gasparich G.E., Gaynor B.J.,
RA   Athey J.C., Harrison N.A., Donofrio N.;
RT   "Complete Genome Sequence of Spiroplasma kunkelii Strain CR2-3x, Causal
RT   Agent of Corn Stunt Disease in Zea mays L.";
RL   Genome Announc. 3:e01216-e01215(2015).
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; CP010899; ALA97075.1; -; Genomic_DNA.
DR   RefSeq; WP_053390426.1; NZ_CP010899.1.
DR   AlphaFoldDB; A0A0K2JEQ9; -.
DR   STRING; 273035.SKUN_00151; -.
DR   KEGG; skn:SKUN_00151; -.
DR   PATRIC; fig|273035.7.peg.176; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000062963; 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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   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          600..940
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         256..283
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         743..769
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         644..651
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   950 AA;  105664 MW;  9175E14D59AEADA6 CRC64;
     MGKDWIVVKG ARENNLKNID VKVPKDKLVV FTGLSGSGKS SLAFNTIYAE GRRRYIESLS
     SYARQFLGGN EKPDVDAIEG LSPAISIDQK TTSHNPRSTV GTVTEIYDYL RLLYARVGTP
     YCINGHGVIK SVTVKEIINN LKQLLTEGEK FMILSPVVRY KKGSFKDLFA RLKQESFIRV
     KVNDEIKTLD EEIELDKNKQ QNIDIIIDRL VYKESADLLS RIHDAIEVAL KYGNALVKID
     FADQKKEMLF STNYSCSICG FVIPELEPRL FSFNSPSGAC SECKGLGVKL EVDEDLLIPN
     RSLSILQGAI IYLKNIVNTT NIEWQKFKVL ANYYHIVLEQ PVSDLTKEQL EYLIRGSDEP
     IEYNLKTASG NIMRGYDYIE GIGQLIERRY TETSSESQRE YYKQFMTDKK CGTCLGKRLN
     EIPLSVKINN ISISEFTDLS VEDELKEVLN LKLTESQQEI ARLIINELVN RLDFLSRVGL
     GYLTLSRNAS TLSGGEAQRI RLATQIGSQL TGVLYVLDEP SIGLHQRDND KLIETLKNLR
     DLGNTLIVVE HDEDTIRASD YIIDIGPRAG INGGQVVAAG SIDDIQQNPN SITAKYLTGE
     LAIDVPKKRR GGNGLVLEIK GARENNLKNI NVTIPLNKFV CLTGVSGSGK STLMNEILWK
     GIKKNLGLAT ERPGAHDKIL GIDNIDKVIN ISQDPIGKTP RSNPATYTSV FDDIRDLFAD
     TNEAKARGYL KGRFSFNVPG GRCEHCQGDG IIKISMHFLP TVYVSCEVCE GKRYNDETLL
     VKFKDKNIYD VLEMTVDQAC DFFATQPKIS QKLGTMQEVG LGYIKLGQSA TELSGGEAQR
     VKLSTFLLKR TTGKTLFLLD EPTTGLHVDD VNRLLVVLNK IVDNGDTVIT IEHNLDVIKM
     ADYIIDLGPE GGVGGGMIVA TGTPEQLVLK SGTSYTAQYL KPLLKSKRLE
//
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