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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//