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Database: UniProt
Entry: A0A1M5HII9_9FLAO
LinkDB: A0A1M5HII9_9FLAO
Original site: A0A1M5HII9_9FLAO 
ID   A0A1M5HII9_9FLAO        Unreviewed;       929 AA.
AC   A0A1M5HII9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156};
GN   ORFNames=SAMN05444396_105114 {ECO:0000313|EMBL:SHG15632.1};
OS   Flavobacterium segetis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=271157 {ECO:0000313|EMBL:SHG15632.1, ECO:0000313|Proteomes:UP000184036};
RN   [1] {ECO:0000313|Proteomes:UP000184036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19741 {ECO:0000313|Proteomes:UP000184036};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQWE01000005; SHG15632.1; -; Genomic_DNA.
DR   RefSeq; WP_072990929.1; NZ_FQWE01000005.1.
DR   AlphaFoldDB; A0A1M5HII9; -.
DR   STRING; 271157.SAMN05444396_105114; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000184036; 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   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:SF4; 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};
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          591..924
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   929 AA;  104151 MW;  13B96EF2E77421E3 CRC64;
     MQVDLSQLDP KKNIIIKGAQ VHNLKNVDVA IPRNKLVVIT GLSGSGKSSL AFDTLYAEGQ
     RRYVESLSSY ARQFLGRLDK PKVEYIKGIA PAIAIEQKVN TTNARSTVGT STEIYDYIKL
     LFARIGRTYS PVSGREVKKN TVTDVVTDVK TFDLDSKWLL LAPIHLEEGR KLEDKLKVLL
     QQGFARILVN NEMIRLDDLP DSLDKNDILL IVDRIVVKEE EEFYNRLADA VQTAFFEGKG
     ICYLQELNAD KKYTYSNNFE LDGITFLEPN VHLFSFNNPY GACPICEGYG NIIGIDAELV
     IPNTTLSVFE NAIFPWRGES MSYYRDELVN KAYKFDFPIH KPFFQLSEDQ KELIWSGNQY
     FQGLNAFFKE LEEKNYKIQN RVMLSRYRGK TKCYSCKGKR LRVEASYVKI NSKTVSDLVD
     LPIKHLVTFF QNIDLNVYEK QIAKRLLLEI NNRLSFLTEV GLDYLTLNRN SATLSGGESQ
     RINLATSLGS SLVGSMYILD EPSIGLHPKD TERLIKVLLS LRDLGNTVIV VEHDEDIMKA
     ADMIIDIGPE AGTLGGNLVA QGSYEEILKS TSLTAKYLNG DLEISVPKKR RTFKNYIEIK
     GARENNLQNI DVTFPLDVLT VITGVSGSGK STLVKKILFP AMQKKLENIG EKAGQFSEIS
     GSFSQIKHIE YVDQNPIGRS SRSNPVTYIK AYDDIRELYA REKLSKIRGY QAKHFSFNVD
     GGRCETCKGE GSINVEMVFM ADVQLPCETC NGKRFKKEVL EVAFEGKNIN DILTMTVDDA
     IAFFTAQKQA KIIQKLQPLQ DVGLGYVQLG QSSSTLSGGE AQRIKLASFL VKGVTKEKAL
     FVFDEPTTGL HFHDIKKLLK SFDALIEKGH SIIVIEHNLD LIKCADWVID LGPEGGENGG
     KLLAVGTPEE IVKNKKSVTA TYLKAALKK
//
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