ID G0HAJ0_CORVD Unreviewed; 948 AA.
AC G0HAJ0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=uvrA1 {ECO:0000313|EMBL:AEK36597.1};
GN Synonyms=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN OrderedLocusNames=CVAR_1241 {ECO:0000313|EMBL:AEK36597.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36597.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK36597.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
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; CP002917; AEK36597.1; -; Genomic_DNA.
DR RefSeq; WP_014009783.1; NC_015859.1.
DR AlphaFoldDB; G0HAJ0; -.
DR STRING; 858619.CVAR_1241; -.
DR GeneID; 82887051; -.
DR KEGG; cva:CVAR_1241; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_11; -.
DR Proteomes; UP000006659; 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; 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 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 616..945
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 748..774
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 649..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 948 AA; 104194 MW; 613A62C0117CF0CD CRC64;
MAEILTVRGA REHNLKGVDI DLPRDRMIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSS
YARQFLGQMD KPDVELIEGL SPAVSIDQKS TNRNPRSTVG TITEIHDYLR LLFARTGIAH
CPECGARIER QTPQQIVDQV LGMEEGLKFQ VLAPVVRTRK GEFVDLFEDL SAQGYARVLV
DGEAYRLTDP PQLEKQVKHD IDVIVDRLQV KPSQKQRLTE SVETALGLAD GRVVLDFVGL
DDDDPDRRRR FSENMACPNG HALAIDELEP RSFSFNSPYG ACPSCDGLGT KLEVDEALII
PDEDAPLVGA IAPWASSPNH RYFDKLLTAL AENLGVDPDT RWSELTKKER KAVLTGHPEE
ITVRYRNRYG RSRQYSAPFE GVLHYLHRKI DQAESDNQKE RYLGYMREVP CPACGGTRLR
PEILQVTIDS ESGEKSIADV SAMSIEDASS FLDSLTLNSR DEMIAGRVLK EIQARLRFLI
DVGLNYLSMS RAAGTLSGGE AQRIRLATQI GSGLAGVLYV LDEPSIGLHQ RDNTRLIATL
KHLRDIGNTL IVVEHDEETI RTADWLVDIG PRAGEFGGHV VYQGEPEGIL DCAESITGQY
LSGQRILAVP EQRREVDTGR VITVHGATEN NLKNVTVDFP LGVLTCVTGV SGSGKSSLVN
GILAQVLANQ LNGARQVPGH HRKVTGLDQL DKLVRVDQSP IGRTPRSNPA TYTGVFDKIR
NLFAETAEAK VRGYKAGRFS FNVKGGRCEA CHGDGTLKIE MNFLPDVYVP CEVCQGARYN
RETLEVHYKG KSIAEVLDMP ISEAAEFFGP VTSISRYLNT LVDVGLGYVR LGQAATTLSG
GEAQRVKLAS ELQKRSNGRT VYILDEPTTG LHFEDIRKLM LVIQGLVDKG NTVLVIEHNL
DVIKAADWII DMGPEGGAGG GTVVAEGTPE EVARVEASHT GRYLNEML
//
