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Database: UniProt
Entry: A0A387BBK1_9MICO
LinkDB: A0A387BBK1_9MICO
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ID   A0A387BBK1_9MICO        Unreviewed;       967 AA.
AC   A0A387BBK1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
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:AYF99068.1};
GN   ORFNames=D7I47_12915 {ECO:0000313|EMBL:AYF99068.1};
OS   Protaetiibacter intestinalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Protaetiibacter.
OX   NCBI_TaxID=2419774 {ECO:0000313|EMBL:AYF99068.1, ECO:0000313|Proteomes:UP000278886};
RN   [1] {ECO:0000313|Proteomes:UP000278886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2DFWR-13 {ECO:0000313|Proteomes:UP000278886};
RA   Heo J., Kim S.-J., Kwon S.-W.;
RT   "Genome sequencing of strain 2DFWR-13.";
RL   Submitted (SEP-2018) 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; CP032630; AYF99068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A387BBK1; -.
DR   KEGG; lyd:D7I47_12915; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000278886; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000278886};
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          617..951
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         754..780
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         655..662
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   967 AA;  106119 MW;  402DDCF2BF02CD0F CRC64;
     MSITPVSGSQ KLSVRGARVH NLKDVDLEIP RDALVVFTGL SGSGKSSLAF DTIFAEGQRR
     YVESLSAYAR QFLGQVDRPD VDFIEGLSPA VSIDQKSTNR NPRSTVGTIT EIYDYMRLLW
     ARIGEPHCPV CGERIQRQTV QQIADQLMEL PTGTRYQVLA PVVSQKKGEF VDLFKELSAS
     GYSRAIVDGE LVQLAEPPAL KKQYKHDIAV VIDRLVASDE LLTRVTDSVE TALGLAGGVL
     EIDFVDEEPT AKTRRRSFSE KLSCPNGHPI QLTEIEPRTF SFNAPFGACP ECSGLGTKMA
     VDTDLVIGDP ELSLNEGVIL PWNQGGKGLY SYFQRLLQGL ARDLDFSLDT PWGELPDEVR
     AAILQGNDFE VVVQWRNRFG RTMKYSTGFE GVMPYIERKY HEAESDWSQQ RYGEYLREVP
     CPVCAGKRLK PEVLAVRVAG ESISDVAELS LVTAYEFMQR LELTEREARI AAQVLREIRL
     RLEFLLEVGL GYLTMARAAA TLSGGEAQRI RLATQIGSGL TGVLYVLDEP SIGLHQRDNR
     RLIDTLVKLK SLGNTLIVVE HDEDTIRTAD WIVDIGPGAG EHGGRVVHSG GYEALLDNHA
     SVTGDYLAGR RAIAMPAKRR PIDKKRQLTV EGAQANNLQN VTVSFPLGAF VAVTGVSGSG
     KSSLVNDILY KVLANQLNGA RQVPGKHKRV TGLEHLDKVV HVDQAPIGRT PRSNPATYTG
     VFDRIRTLFS ETIEAKARGY QPGRFSFNVK GGRCENCSGD GTIKIEMNFL PDVYVVCEVC
     HGARYNRDTL QVHYKGKNIA EVLDMPIAEA AEFFEPITAI HRYLKTLVDV GLGYVRLGQS
     ATTLSGGEAQ RVKLATELQK RSNGRSIYVL DEPTTGLHFE DVRKLLEVLN GLVDKGNSVI
     VIEHNLDVIK SADWIIDLGP EGGSGGGQVI ATGTPEQVAR NAASHTGRFL AELLESEAAG
     RGRRKAG
//
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