ID F8J552_HYPSM Unreviewed; 1000 AA.
AC F8J552;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
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 ECO:0000313|EMBL:CCB64570.1};
GN OrderedLocusNames=HYPMC_1339 {ECO:0000313|EMBL:CCB64570.1};
OS Hyphomicrobium sp. (strain MC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB64570.1, ECO:0000313|Proteomes:UP000000494};
RN [1] {ECO:0000313|Proteomes:UP000000494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA Genoscope.;
RT "The complete genome of Hyphomicrobium sp. MC1.";
RL Submitted (MAY-2011) 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 -!- 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; FQ859181; CCB64570.1; -; Genomic_DNA.
DR RefSeq; WP_013946977.1; NC_015717.1.
DR AlphaFoldDB; F8J552; -.
DR STRING; 717785.HYPMC_1339; -.
DR KEGG; hmc:HYPMC_1339; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_5; -.
DR OMA; PFEGIIP; -.
DR Proteomes; UP000000494; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000494};
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 629..970
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT ZN_FING 773..799
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT REGION 972..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT BINDING 674..681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ SEQUENCE 1000 AA; 109874 MW; 60EC2DC7AE1F5CF8 CRC64;
MAKSTKPNSR PASELMKTIH VRGAREHNLK NVDIEIPRDA LVVFTGLSGS GKSSLAFDTI
YAEGQRRYVE SLSAYARQFL EMMQKPDVDH IDGLSPAISI EQKTTSKNPR STVGTVTEIY
DYLRLLFARV GVPYSPATGL PIESQTVAQM VDRVLALPDG TRLLLLAPVV RGRKGEYRKE
IAEWQKKGYQ RLKINGTVYA IEDAPKLDKK YKHDIDVVID RIVVKKDIGT RLADSFEQAL
KLSDGLAIAE YVDKPLSKAE TEGANKSKND THERILFSSR FACPVSGFTI DEIEPRLFSF
NAPAGACPVC DGLGSELRFE PDLVVPDGSL SLEKGAIFPW AKTGVSSPYY EQTLESLAKH
YKISMKTPWE KLPKHVQLAL LFGSGDEDVT FTYWDGTRNY STEKPFEGVI GNIARRFKET
DSDWVREELS RYQAAHPCEG CNGFRLKPQA LAVKIGGKHI GEVCDLSIKA ANVWFSEIPK
TFTKQQSEIA TRILKEIRDR LKFLNDVGLE YLTLSRSSGT LSGGESQRIR LASQIGSGLT
GVLYVLDEPS IGLHQKDNDR LLETLKHLRD IGNTVIVVEH DEDAIMTADH VVDIGPGAGV
HGGKVIAQGT PQDIMDSPQS ITGEYLSGTR FVPVPKNRRA PDPKRMLTVT GARENNLKNV
TASVPVGLFT CITGVSGGGK STLLIDTLFK AVARKLNNAK DHPGEHDKIT GIEHFDKIID
IDQSPIGRTP RSNPATYTGA FTPIREWFAG LPEAKTRGYE PGRFSFNVKG GRCEVCQGDG
VIKIEMHFLP DVYVTCEECK GKRYNRETLA VTFKEKSIAD VLDMTVEEGA EFFKAVPSIR
DKLETLARVG LGYIHIGQQA TTLSGGEAQR IKLSKELSRR ATGRTLYILD EPTTGLHFHD
VAKLLEVLHE LADAGNTVVV IEHNLEVIKT ADWIIDLGPE GGDGGGTIVA AGTPEDIVKV
KESYTGQYLK PVLARSKAAP GGRPPGRESP GANKKRQAAE
//