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Entry: A0A261V0P7_9BORD
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Original site: A0A261V0P7_9BORD 
ID   A0A261V0P7_9BORD        Unreviewed;       950 AA.
AC   A0A261V0P7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=CAL20_00140 {ECO:0000313|EMBL:OZI67495.1};
OS   Bordetella genomosp. 4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463044 {ECO:0000313|EMBL:OZI67495.1, ECO:0000313|Proteomes:UP000216885};
RN   [1] {ECO:0000313|EMBL:OZI67495.1, ECO:0000313|Proteomes:UP000216885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU9919 {ECO:0000313|EMBL:OZI67495.1,
RC   ECO:0000313|Proteomes:UP000216885};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) 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:OZI67495.1}.
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DR   EMBL; NEVQ01000001; OZI67495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261V0P7; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000216885; 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:UP000216885};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
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          602..943
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         251..278
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         31..38
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   950 AA;  104520 MW;  49394BC94CCD6B78 CRC64;
     MNAIRIRGAR THNLKNVSLD LPRHKLVVVT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLQLMDK PDVDLIEGLS PAISIEQKAA GHNPRSTVGT ITEIHDYLRL LYARVGTPYC
     PDHGLPLQAQ SVSQVVDAVL AWPAETRLAV LAPIARARKG SFEDECASLQ AQGYVRLRVD
     GQMQEISDMA PLKKNEKHDI DVVIDRLRIR PESKQRLAES FETAMQLADG RTVALDMDSG
     REQVFSSRYA CPVCSHSLPE LEPRLFSFNN PMGACPSCDG IGQVGFFDPK RVVAFPELSL
     AAGAVRGWDR RNAFTHSLLT SLAAHYEFDI ETPFEELPED VRHKVLYGSG EEEIAFLYLN
     EKGRSTVKRH AFEGIIPNLE RRWRETDSPT VREELGKYRN IKTCPDCGGS RLRAEARHVL
     IGTDPRGGER HGQAIYEVEA MPLSDCLAWF RALTLTGAKQ EIAQRIVREI EARLSFLNNV
     GLNYLSLDRS ADTISGGEAQ RIRLASQIGS GLTGVMYVLD EPSIGLHQRD NDRLIGTLQH
     LRDLGNSVIV VEHDEDMIRL ADWVVDMGPG AGEHGGQVVA QGTPEAVQAD PASLTGQYLS
     GARAIDIPKR RPVNDEQPWL VLEGASGNNL KTVDLRIPAG RLVCVTGVSG SGKSTLVNDT
     LAVAVSRQLH HAQSEPAPYV SLTGLEHFDK IISVDQSPIG RTPRSNPATY TGLFTPIREL
     FAGVPEARTR GYDPGRFSFN VKGGRCEACQ GDGVVKVEMH FLPDMYVPCD VCHGKRYNRE
     TLEIRYRGRN ISEVLDLTVA QALEYFESVP AIARKLHTLM DVGLSYIRLG QSATTLSGGE
     AQRVKLSLEL SRRSTGRTLY ILDEPTTGLH FRDIEMLLQV LNQLVDSGNT VLIIEHNLDV
     IKTADWLVDM GPEGGDGGGM VVATGTPEDV AANPQSHTGH YLGRVLQRSK
//
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