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Database: UniProt
Entry: A0A1H9YNM5_9BACI
LinkDB: A0A1H9YNM5_9BACI
Original site: A0A1H9YNM5_9BACI 
ID   A0A1H9YNM5_9BACI        Unreviewed;       956 AA.
AC   A0A1H9YNM5;
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=SAMN05421676_101236 {ECO:0000313|EMBL:SES70669.1};
OS   Salinibacillus kushneri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX   NCBI_TaxID=237682 {ECO:0000313|EMBL:SES70669.1, ECO:0000313|Proteomes:UP000199095};
RN   [1] {ECO:0000313|EMBL:SES70669.1, ECO:0000313|Proteomes:UP000199095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SES70669.1,
RC   ECO:0000313|Proteomes:UP000199095};
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}.
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DR   EMBL; FOHJ01000001; SES70669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9YNM5; -.
DR   STRING; 237682.SAMN05421676_101236; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000199095; 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};
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          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   956 AA;  107370 MW;  527005DA223DCF95 CRC64;
     MAMKSIKVQG ARAHNLKNVD VNIPKNKLVV MTGLSGSGKS SLAFDTIYAE GQRRYVESLS
     AYARQFLGQM DKPDVDAIEG LSPAISIDQK TTSRNPRSTV GTVTEIYDYL RLLYARVGHP
     YCPEHGIEIT SQTVEQMVDR IMEYPERTKL QILAPVVSGR KGEHAKVFED LRKEGFVRIR
     VDGEMHEVTE DIELDKNKKH SIEVVIDRII VKDGVVSRLS DSIETALKHG DGKVIIDLIG
     DEELLFSEKH ACPICGFSID ELEPRMFSFN SPFGACPTCD GLGTNLEVDV DLVIPDWDLS
     LNEHAIAPWE PSRFQYYPQL LASVCEHYDI PMDVPVKDIP KEKMNKILYG SGKERIHFQY
     TNDRGQARDN HIYFEGVIRN VERRYRESTS DWVREQMEKY MVHKSCPTCH GHRLSEEALS
     VKIDEKHISH VTDYSISEAR EFFQGLKLSE KEEQIAQMIL KEISDRLTFL QNVGLDYLTL
     SRSAGTLSGG EAQRIRLATQ IGSALTGVLY VLDEPSIGLH QRDNNRLIAT LQQMRDLDNT
     LIVVEHDEDT MLEADYIIDI GPGAGSHGGE LVASGTPKQV MRSRNSLTGQ YLSGKKFIPL
     PNERRNPNNR FIEIVGAEEN NLKNVDVQIP LGLLNVVTGV SGSGKSSLIN EILYKSLSQK
     LYKSKLKPGK YKEINGLDHL DKVIDIDQSP IGRTPRSNPA TYTGVFDDIR DVFAQTNEAK
     IRGYKKGRFS FNVKGGRCEA CHGDGIIKIE MHFLPDVYVP CEVCHGKRYN RETLEVKYKG
     KTIADVLDMR VEEALDFFEN IPKIKRKIQT IADVGLGYIK LGQPATTLSG GEAQRMKLAS
     ELHRRSNGKS FYILDEPTTG LHVHDIKQLL TVLQRLVENG DTVLIIEHNL DVIKTADYLI
     DLGPEGGEGG GKIVATGAPE EVADQEDVSY TGKYLKPILE RDRKRMDERL NEKVTS
//
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