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Database: UniProt
Entry: A0A3M2I483_9GAMM
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ID   A0A3M2I483_9GAMM        Unreviewed;       959 AA.
AC   A0A3M2I483;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:RMH94419.1};
GN   ORFNames=EBB59_01620 {ECO:0000313|EMBL:RMH94419.1};
OS   Lysobacter pythonis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=2483112 {ECO:0000313|EMBL:RMH94419.1, ECO:0000313|Proteomes:UP000275012};
RN   [1] {ECO:0000313|EMBL:RMH94419.1, ECO:0000313|Proteomes:UP000275012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4284/11 {ECO:0000313|EMBL:RMH94419.1,
RC   ECO:0000313|Proteomes:UP000275012};
RA   Hans-Juergen B., Huptas C., Sandra B., Igor L., Joachim S., Siegfried S.,
RA   Mareike W., Peter K.;
RT   "Proposal of Lysobacter pythonis sp. nov. isolated from royal pythons
RT   (Python regius).";
RL   Submitted (OCT-2018) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMH94419.1}.
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DR   EMBL; RFLY01000002; RMH94419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2I483; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000275012; 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:UP000275012};
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          613..943
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         260..287
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         746..772
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         647..654
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   959 AA;  105958 MW;  6BC84C01E33036BB CRC64;
     MALDTIRIRG ARTHNLKNFD LDLPRDKLIV ITGLSGSGKS SLAFDTIYAE GQRRYVESLS
     AYARQFLSVM EKPDLDHIEG LSPAISIEQK STSHNPRSTV GTITEVYDYL RLLYARVGIP
     RCPDHHFPLE AQTVSQMVDQ VLALAGDPGS SGQRFMLLAP VVRERKGEHA QVFEQLRAQG
     YVRVRVDGDL HEIDAVPPLA LRQKHTIEAV IDRFKVREDM QQRLAESFET ALKLGEGMAI
     VRSLDDARAE PLLFSSKYSC PVCDYALPEL EPRLFSFNAP MGACETCDGL GVAQFFDPAR
     VVTHPELSLA AGAVRGWDRR NTYYFQMLQS LAKHYGFKVD TPWQALPEYI RQAVLHGSGE
     ENIAFTYLND AGSRTTRKHR FEGIIPNLER RYRDTESNAV REELAKYISE RPCPDCNGAR
     LNRAARNVFV GERPIHEVTQ QPIDEALAFF STLKLPGWRG EIAAKIVKEI GERLGFLVDV
     GLDYLTLERK ADTLSGGEAQ RIRLASQIGA GLVGVMYVLD EPSIGLHQRD NERLLGTLTR
     LRDLGNTVIV VEHDEDAIRL ADHVVDIGPG AGVHGGEVIA QGDVKAIIAS ERSLTGDYLS
     GRKAIEIPAK RHAPSKKFML KLKGASGNNL RNVDLEIPAG LMTAITGVSG SGKSTLINDT
     LYALAANEIN GASHTPAAHK EIKGLDLFDK VVDIDQSPIG RTPRSNPATY TGLFTPLREL
     FSQVPEARAR GYAPGRFSFN VRGGRCEACQ GDGLIKVEMH FLPDVYVPCD VCGGKRYNRE
     TLEIVYKGHS IHDVLEMTVE DAAKLFENVP AISRKLDTLI DVGLAYIKLG QSATTLSGGE
     AQRVKLSKEL SRRDTGRTLY ILDEPTTGLH FADIEHLLTV LHRLRDEGNT VVVIEHNLDV
     IKTADWIVDL GPEGGHRGGE IIATGTPETL AQLPHSHTGR FLAKQMEEDA RRAKHRKNA
//
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