ID   A0A2S7WN34_9FLAO        Unreviewed;       940 AA.
AC   A0A2S7WN34;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156};
GN   ORFNames=BTO18_07475 {ECO:0000313|EMBL:PQJ79018.1};
OS   Polaribacter porphyrae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1137780 {ECO:0000313|EMBL:PQJ79018.1, ECO:0000313|Proteomes:UP000238882};
RN   [1] {ECO:0000313|EMBL:PQJ79018.1, ECO:0000313|Proteomes:UP000238882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108759 {ECO:0000313|EMBL:PQJ79018.1,
RC   ECO:0000313|Proteomes:UP000238882};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000256|ARBA:ARBA00038000}.
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:PQJ79018.1}.
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DR   EMBL; MSCN01000001; PQJ79018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7WN34; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000238882; 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-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
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   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; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238882};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          314..589
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          604..936
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   940 AA;  105256 MW;  DD86B0A12D42A359 CRC64;
     MEDQEYIEVY GARAHNLKNI DVKIPREKLV VITGLSGSGK SSLAFDTIYA EGQRRYIETF
     SAYARQFLGG LERPDVDKID GLSPVISIEQ KTTNKSPRST VGTITEIYDF LRLLFARAAD
     AYSYNTGEKM VSYSDEQIKQ LILKDFDNKK VAVLAPLIKS RKGHYRELFE QISKQGFVRV
     RVDGEIKEIE KGMRLDRYKT HDIEVVIDRL LVNKSSEKRL EETIKTALYS GNNIMMVIAI
     DDEKPRYFSR ELMCPTTGIA YPNPEPNTFS FNSPKGACNT CNGLGITNEI NLNKVIPDDS
     KSIKNGGIIP LGEQKNSWIF KQLQNIAERY RFKLTDAIKD IPKEALNVIL NGGNESFKIT
     SKAAGVTRNY KIDFEGIVAF IENQYNSAES TSIKRWAKGF MDEVSCSTCD GKRLKKEALH
     FKITDKNISE LAQMDVTELA KLFANIEENL SEKQNTIASE ILKEIRTRIQ FLLDVGLDYL
     TLDRTSKSLS GGEAQRIRLA TQIGSQLVGV LYILDEPSIG LHQRDNQKLI DSLVKLRDVG
     NSVLVVEHDE DMMKKADYVL DIGPGAGKHG GEIVSIGTYD EIIKNKTLTT DYLTGKRKIE
     VPKKRREGNG KTIKLKGASG NNLKNVSVEF PLGKMICVTG VSGSGKSTLI NETLYPILNA
     HIYRGVKKPM PYKKIEGLEN VDKVIDIDQS PIGRTPRSNP ATYTKTFDEI RSLFAKTPEA
     AIRGYKPGRF SFNVKGGRCE TCQGGGVRVI EMNFLPDVHV ECETCQGKRF NRETLEIRYK
     GKSISDILNM TIEDATDFFE MIPKIHRKLK TIKDVGLGYI TLGQQSTTLS GGEAQRIKLA
     SELSKRDTGN TFYILDEPTT GLHFEDIRVL MEVLNKLANK GNTVLIIEHN LDVIKLADYI
     IDVGMEGGKN GGKIIVKGTP EQVAKHKTSY TAKFLKKELI
//