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Database: UniProt
Entry: F8J552_HYPSM
LinkDB: F8J552_HYPSM
Original site: F8J552_HYPSM 
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
//
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