ID A0A157RQW8_9BORD Unreviewed; 955 AA.
AC A0A157RQW8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=uvrA2 {ECO:0000313|EMBL:SAI68512.1};
GN Synonyms=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN ORFNames=SAMEA3906487_01305 {ECO:0000313|EMBL:SAI68512.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI68512.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI68512.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI68512.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-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; LT546645; SAI68512.1; -; Genomic_DNA.
DR RefSeq; WP_033535210.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157RQW8; -.
DR STRING; 123899.SAMEA3906487_01305; -.
DR GeneID; 56591403; -.
DR KEGG; btrm:SAMEA390648701305; -.
DR PATRIC; fig|123899.6.peg.1280; -.
DR eggNOG; COG0178; Bacteria.
DR OrthoDB; 9809851at2; -.
DR Proteomes; UP000076825; Chromosome 1.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000076825};
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 617..947
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 255..282
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT ZN_FING 750..776
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 651..658
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 955 AA; 104837 MW; 2DA6BFBE7AB04133 CRC64;
MNERTDEIRI RGARTHNLKS VSLDLPRHRL VVITGLSGSG KSSLAFDTLY AEGQRRYVES
LSAYARQFLQ LMDKPDVDLI EGLSPAIAIE QKAAGHNPRS TVGTITEIHD YLRLLYARVG
TPYCPEHGLP LQAQSVAQMV DAVLAWPADT RLAILAPIAR ARKGSFEDEC ASLQAQGYVR
LRVDGQMVEI DQMAPLKKTE KHDIDVVVDR LRVRAESKQR LAESFETALQ LADGRAIALG
MDDGHEQVFS SRYACPVCSH SLPELEPRLF SFNNPLGACP SCDGIGQVGF FDPKRVVAFP
ELSLAAGAIR GWDKRNAFTH SLLTSLATHY EFDIEAPFES LAPEVRDKVL YGSGDEEIAF
FYLNEKGRSS VKRHAFEGVI PNLERRWRET DSATVREELG KYRNIKTCPD CAGSRLRADA
RHVLIGDEPG RHEERGLAIY QVEAMPLSAC LAWFQALQLT GAKQEIAQRI VREIEARLSF
LNNVGLTYLS LDRSADTISG GEAQRIRLAS QIGSGLTGVM YVLDEPSIGL HQRDNDRLIG
TLQHLRDLGN SVIVVEHDED MIRQADWVVD MGPGAGEHGG QVVAQGAPEA IQTDPASLTG
QYLSGARAIA IPQRRPVNDE QPWLVLSGAS GNNLKSVTLR VPAARLVCVT GVSGSGKSTL
VNDTLAVAAA RQLNHAQGEP APYASITGLE HFDKIITVDQ SPIGRTPRSN PATYTGLFTP
IRELFAGVPE ARTRGYDPGR FSFNVKGGRC ESCQGDGVVK VEMHFLPDMY VPCDVCHGKR
YNRETLEIRY RGRNISEVLD LTVEQALDYF ESVPAIARKL QTLIDVGLSY IRLGQSATTL
SGGEAQRVKL SLELSRRSTG RTLYILDEPT TGLHFRDIEL LLQVLNQLVE QGNTVLIIEH
NLDVIKTADW LIDMGPEGGN KGGQVVAQGT PETVAAHPDS HTGHYLARLL PTPGR
//
