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Database: UniProt
Entry: A0A3N3ZUZ3_9MICC
LinkDB: A0A3N3ZUZ3_9MICC
Original site: A0A3N3ZUZ3_9MICC 
ID   A0A3N3ZUZ3_9MICC        Unreviewed;       967 AA.
AC   A0A3N3ZUZ3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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:ROZ63817.1};
GN   ORFNames=EDL96_05615 {ECO:0000313|EMBL:ROZ63817.1};
OS   Kocuria soli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=2485125 {ECO:0000313|EMBL:ROZ63817.1, ECO:0000313|Proteomes:UP000270616};
RN   [1] {ECO:0000313|EMBL:ROZ63817.1, ECO:0000313|Proteomes:UP000270616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M5W7-7 {ECO:0000313|EMBL:ROZ63817.1,
RC   ECO:0000313|Proteomes:UP000270616};
RA   Tuo L.;
RT   "Kocuria sp. M5W7-7, whole genome shotgun sequence.";
RL   Submitted (OCT-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROZ63817.1}.
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DR   EMBL; RKMF01000005; ROZ63817.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N3ZUZ3; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000270616; Unassembled WGS sequence.
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:UP000270616};
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          631..960
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         763..789
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         664..671
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   967 AA;  106794 MW;  F5DBB2FA9B017008 CRC64;
     MLTVPEAQAT APTDLTEIVV QGAREHNLHD VDLTIPRDAM VVFTGLSGSG KSSLAFDTIF
     AEGQRRYVES LSSYARMFLG RVDKPDVDFI EGLSPAVSID QKSTSKNPRS TVGTITEIYD
     YMRLLWARIG HPHCPVCGEP ITKQTPQQIV DRLLTMPERT RFQVLAPVVR RRKGEFADLF
     ASLTQQGYSR AVVDGEQVTL DDPPKLKKQY KHDIDVVVDR LVIKDGMERR LTDSIETALG
     LADGRVVVEL VLRDGEDAPE GIDQRQTFSE NLACPNEHPL GTDEIEPRAF SFNAPFGACP
     ECDGIGTRLE VDEHLVVPDP DLSLVEGAIQ PWSLGKSTSD YWNRLMAGLG EELDFDLVTP
     WKDLPAAGRK ALLEGKDYKV TVSYRNRWGR ERRYTQGFEG VYTYIRRKHE ETESENAKDR
     YEQYMRQVPC PACQGQRLNP TMLGVTVGGL SIAQATALPM RESLAFFQGL ELTERETRIA
     EQVLKEIEAR LTFLLDVGLD YLNLERASAT LSGGEAQRIR LATQIGAGLV GVLYVLDEPS
     IGLHQRDNRR LIQTLTKLRD MGNTLIVVEH DEDTIREADW IVDVGPGAGE RGGRVVHSGG
     YQELLANKDS ITSDYLSGRK AIDVPATRRP VDPERVLRVV GAQENNLQNI DVTFPLGVFT
     AVTGVSGSGK SSLVNEILYT KLANELNGAK QVPGRHKRIE GVEQLKKIVH VDQSPIGRTP
     RSNPATYSGV FDRIRKLFAD TPEAKIRGYQ PGRFSFNVKG GRCEACSGDG TLKIEMNFLP
     DVYVPCEVCK GARYNRETLD VHYKGKSIAE VLDMPIEEAA EFFSAYTAIA RHLDTLVDVG
     LGYVRLGQPA TTLSGGEAQR VKLAAELQRR SHGDTIYVLD EPTTGLHFED INKLLKVLQG
     LVDKGNSVMT IEHNLDVIKT ADWVIDMGPD GGSGGGLVVA EGTPEDVAQN PASHTGMFLK
     EIFEGAR
//
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