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Database: UniProt
Entry: A0A1I6LKN3_9MICO
LinkDB: A0A1I6LKN3_9MICO
Original site: A0A1I6LKN3_9MICO 
ID   A0A1I6LKN3_9MICO        Unreviewed;       965 AA.
AC   A0A1I6LKN3;
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=SAMN04487846_1738 {ECO:0000313|EMBL:SFS04016.1};
OS   Microbacterium sp. cf046.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1761803 {ECO:0000313|EMBL:SFS04016.1, ECO:0000313|Proteomes:UP000199422};
RN   [1] {ECO:0000313|EMBL:SFS04016.1, ECO:0000313|Proteomes:UP000199422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF046 {ECO:0000313|EMBL:SFS04016.1,
RC   ECO:0000313|Proteomes:UP000199422};
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; FOZJ01000002; SFS04016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LKN3; -.
DR   STRING; 1761803.SAMN04487846_1738; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000199422; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199422};
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          624..953
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         756..782
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         657..664
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   965 AA;  105913 MW;  D4A981EDB2177744 CRC64;
     MPIVPVAAPG NSSGRLSVRG ARVHNLKNVD LDIPRDSLVV FTGLSGSGKS SLAFDTIFAE
     GQRRYVESLS AYARQFLGQV DRPDVDFIEG LSPAVSIDQK STNRNPRSTV GTITEIHDYM
     RLLWARIGVP HCPECGEVIQ RQTVQQIADQ LMELPEKTRY QIVAPVVSQK KGEFVDLFKE
     LSAKGYARAV VDGELVQLAE PPALKKSYKH DIAVVVDRLV ASPEILSRVT DSVETAIGLA
     GGIVQVNFVD EEGDAAWQSF SEKLACPNGH PLQLTEIEPR TFSFNAPFGA CPTCSGLGTR
     MSVDVDLMLG DEEASIREGV LIPWTTQGKG LFQYYERLLE GLAADLNFSL DTPWRDLRLD
     VQEAVLRGEN YKVTVKWKNR YGREMRYSSG FEGVVPYIER QYVQADSDSQ RQRWSEYLRE
     VPCLACNGDR LKPEVLAVLV HGHSIADASR LSLADAQEYF AQLELTEREA KIAAQVLREI
     RARLNFLLQV GLNYLSLSRS AGSLSGGEAQ RIRLATQIGS GLTGVLYVLD EPSIGLHQRD
     NRRLIETLLT LRDLGNTLIV VEHDEETIHA ADWVVDIGPR AGVDGGHVVH SGPLSELLND
     TRSITGDYLS GRRSIPTPAK RRRIDKKRML TVVGARENNL RNVTVDFPLG VMTAVTGVSG
     SGKSSLVNGI LYEVLATRLN GARRIAGKHT RVTGLDNLDK VVHVDQAPIG RTPRSNPATY
     TGVFDRVRTL FSETPEAKAR GYQPGRFSFN VKGGRCEACS GDGTIKIEMN FLPDVYVDCE
     VCHGKRYNRD TLSVHYKGKN IAEVLEMPIE EAAEFFEPIQ AIHRYLKTLV DVGLGYVRLG
     QSATTLSGGE AQRVKLATEL QRRSNGRSVY VLDEPTTGLH FEDVQRLLEV LNSLVEKGNT
     VIVIEHNLDV IKSSDWIIDL GPEGGSGGGE VVATGTPEQV ARAEGSHTGA FLAEVLGLSA
     VRKAG
//
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