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Database: UniProt
Entry: A0A385NVV1_9BACI
LinkDB: A0A385NVV1_9BACI
Original site: A0A385NVV1_9BACI 
ID   A0A385NVV1_9BACI        Unreviewed;       959 AA.
AC   A0A385NVV1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=DOE78_22245 {ECO:0000313|EMBL:AYA77902.1};
OS   Bacillus sp. Y1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=352858 {ECO:0000313|EMBL:AYA77902.1, ECO:0000313|Proteomes:UP000265711};
RN   [1] {ECO:0000313|EMBL:AYA77902.1, ECO:0000313|Proteomes:UP000265711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y1 {ECO:0000313|EMBL:AYA77902.1};
RA   Rathod J., Jean J.-S.;
RT   "Arsenic resistant and redox active subsurface bacterial isolate Bacillus
RT   sp. Y1 from Yichu borehole sediment.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP030028; AYA77902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A385NVV1; -.
DR   KEGG; bacq:DOE78_22245; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000265711; 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; 2.
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:UP000265711};
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          329..593
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          604..935
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         738..764
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         639..646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   959 AA;  107238 MW;  D3F5C6700BA5E989 CRC64;
     MAMEKLIVKG ARAHNLKDID VTIPRDKLVV LTGLSGSGKS SLAFDTIYAE GQRRYVESLS
     AYARQFLGQM DKPDVDMIEG LSPAISIDQK TTSRNPRSTV GTVTEIYDYL RLLYARVGRP
     TCPNHGIEIS SQTIEQMVDR IMEYPERTKL QVLAPIVSGR KGTHVKVFED IKKQGFVRVR
     VDGEMLDLSD EIELEKNKKH TIEVVVDRIV VKEGVTARLA DSLETALGLG EGKVIIDVIG
     EEELLFSEHH ACPLCGFSIT ELEPRMFSFN SPFGACPDCD GLGSKLEVDV DLVVPNKELS
     LKQHAIAPWE PTSSQYYPQL LEAVCNHFGI DMNIPVKDIP KHLFEKVLFG SKEDDIYFRY
     ENDFGQIREG YIQFEGVIRN VERRYKETSS DFIREQMEKY MAQHHCPTCK GDRLKKETLA
     VLINNHHIGK VTSFSIQEAN NFFDHLDLTE KETKIANLIL REIKERLGFL INVGLDYLTL
     NRAAGTLSGG EAQRIRLATQ IGSRLTGVLY ILDEPSIGLH QRDNDRLIDT LKNMRDIGNT
     LIVVEHDEDT MLAADYLIDV GPGAGVHGGQ IVSAGTPQEV MDDPNSLTGQ YLAGKKFIPL
     PIERRKSDGR YVEIKGAKEN NLNNVNVKFP LGMFIAVTGV SGSGKSTLIN EILHKSLAQK
     LNRAKTKPGE HREIKGIEHL DKVIDIDQSP IGRTPRSNPA TYTGVFDDVR DVFAATNEAK
     VRGYKKGRFS FNVKGGRCEA CRGDGIIKIE MHFLPDVYVP CEVCHGKRYN RETLEVKYKG
     KNISDVLDMT VEDALVYFEN IPKIKRKLQT IHDVGLGYIT LGQPATTLSG GEAQRVKLAS
     ELHRRSTGRS FYILDEPTTG LHVDDISRLL VVLQRLVENG DTVLVIEHNL DVIKAADYII
     DLGPEGGDKG GTIIAMGTPE QVAEVPISYT GKYLKPILDR DRERMKKQIQ QKEEQVTNV
//
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