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Database: UniProt
Entry: A0A238XZ42_9FLAO
LinkDB: A0A238XZ42_9FLAO
Original site: A0A238XZ42_9FLAO 
ID   A0A238XZ42_9FLAO        Unreviewed;       941 AA.
AC   A0A238XZ42;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156};
GN   ORFNames=SAMN06265371_107178 {ECO:0000313|EMBL:SNR64316.1};
OS   Lutibacter agarilyticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1109740 {ECO:0000313|EMBL:SNR64316.1, ECO:0000313|Proteomes:UP000198384};
RN   [1] {ECO:0000313|EMBL:SNR64316.1, ECO:0000313|Proteomes:UP000198384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29150 {ECO:0000313|EMBL:SNR64316.1,
RC   ECO:0000313|Proteomes:UP000198384};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; FZNT01000007; SNR64316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238XZ42; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000198384; 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:UP000198384};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          321..596
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          597..937
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   941 AA;  105645 MW;  1BB97AE2FC5C7E21 CRC64;
     MTKHEEYIEV LGARVHNLKN IDVRIPREKL VVITGLSGSG KSSLAFDTIY AEGQRRYIET
     FSAYARQFLG GLERPDVDKI DGLSPVISIE QKTTNKSPRS TVGTITEIYD FLRLLYARAA
     DAYSYNTNKK MVSYSDEQIK ELILKTYEGK KIVILAPVIK SRKGHYRELF DQIAKQGFVK
     VRVDGEIVDI EKGMRLDRYK THDIEIVIDR IAISENSDKR LEETINTALY TGENILMVLE
     HNTNSPRYFS RDLMCPETGI SYPNPEPNTF SFNSPKGACD SCNGLGITNS VNIDKIIPNK
     NISIKNGGIA PLGEQKSSWI FKQLQLIADR YKFQLTDSIS EIPKEALEII LNGGQEKFKI
     TSKTVGVTRS YEIDFEGIIN FINNQYKSTD STSIKRWAKD FMDEIECGSC NGARLKKEAL
     YFKFNEKNIS ELAQMDITEI ANWFSKIEEK LSNKQLKIAS EILKEIRTRI QFLLDVGLDY
     LTLDRSSKSL SGGEAQRIRL ATQIGSQLVG VLYILDEPSI GLHQRDNEKL IKSLINLRDV
     GNSVIVVEHD KDMIEQADYV IDIGPGAGVH GGEIVSEGTF KELKKHHTLT ADYLNGTKKI
     EVPKKRREGN GKKITLKGAT GNNLKNISVD FPLGQLICVT GVSGSGKSTL INETLYPILN
     KHIYRGIKKP MPYKSIKGLE HIDKVIAIDQ SPIGRTPRSN PATYTGVFGE IRSLYAKTNE
     ASIRGYKPGR FSFNVKGGRC ETCQGGGVRV IEMNFLPDVQ VECETCQGKR FNRETLEIRY
     KGKSISDVLN MTIEESVTFF EHIPKIYRKL KTINDVGLGY ISLGQQSTTL SGGEAQRIKL
     AAELSKRDTG NTFYILDEPT TGLHFEDIRV LMEVLNKLTN KGNTILVIEH NMDVIKLADY
     IIDIGMEGGK NGGQLICYGT PEEVSKHKTS YTSKFLKKEL H
//
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