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Database: UniProt
Entry: A0ZBW7_NODSP
LinkDB: A0ZBW7_NODSP
Original site: A0ZBW7_NODSP 
ID   A0ZBW7_NODSP            Unreviewed;       956 AA.
AC   A0ZBW7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 98.
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   ORFNames=NSP_11880 {ECO:0000313|EMBL:AHJ27529.1};
OS   Nodularia spumigena CCY9414.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Nodularia.
OX   NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ27529.1, ECO:0000313|Proteomes:UP000019325};
RN   [1] {ECO:0000313|EMBL:AHJ27529.1, ECO:0000313|Proteomes:UP000019325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ27529.1};
RX   PubMed=23555932;
RA   Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA   Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA   Stal L.J., Hess W.R.;
RT   "Insights into the physiology and ecology of the brackish-water-adapted
RT   Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT   analysis.";
RL   PLoS ONE 8:E60224-E60224(2013).
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}.
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DR   EMBL; CP007203; AHJ27529.1; -; Genomic_DNA.
DR   RefSeq; WP_006194931.1; NZ_CP007203.1.
DR   AlphaFoldDB; A0ZBW7; -.
DR   STRING; 313624.NSP_11880; -.
DR   GeneID; 78016526; -.
DR   PATRIC; fig|313624.11.peg.1188; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_3; -.
DR   Proteomes; UP000019325; 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; 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};
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..945
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         273..300
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         748..774
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         649..656
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   956 AA;  105593 MW;  908602E2AF44F1A1 CRC64;
     MSDHKLARSL SHHHSQNTIR IRGARQHNLK NIDLELPRDR LIVFTGVSGS GKSSLAFDTI
     FAEGQRRYVE SLSAYARQFL GQLDKPDVEA IEGLSPAISI DQKSTSHNPR STVGTVTEIY
     DYLRLLFGRA GEPHCPICDR SIAPQTIDEM CDRISDLPDR TKFQILAPVV RGKKGTHRKL
     ISSLASQGFV RVRVDGEVRE LSDSIELDKN ITHTIEVVID RLVKKAGIQE RLVDSLSTCL
     KQSGGIATIL VSVTSDSGED TEEELVFSEN FACPVHGAVM EELSPRLFSF NSPYGACPHC
     HGIGTLKTFT PDLIVPDPDA PIYAAIAPWS EKDNSYYLEL LYSVGQSTGF ELQAKWNQLT
     VEQQHTVMYG EKEKRTAEAQ RTQSFKGVIP ILQRQYEGGT ELVKQKLEQY LVDQPCEVCG
     GKRLKPEALA VRLGQYGILD LTGVSIQDCR ERIDLLELGD RQIQIADLVL REIKARLQFL
     LDVGLDYLTL DRPAMTLSGG EAQRIRLATQ IGSGLTGVLY VLDEPSIGLH QRDNGRLLKT
     LTKLRDLGNT LIVVEHDEET IRAANYIVDI GPGAGIHGGN IVSQGDLETL LAAEDSLTGA
     YLSGRRVITT PQERRKGNGR SLVIKNAHRN NLRNIDVEIP LGKLVAVTGV SGSGKSTLIN
     ELLYPSLQHH LTKKIPLPRH LQEIQGLNAV DKAIVIDQSP IGRTPRSNPA TYTGIFDAIR
     DVFSQTVEAK ARGYKPGQFS FNVKGGRCEA CSGQGVNVIE MNFLPDVYVQ CEVCKGARYN
     RETLQVKYKD KSISDVLNMT VEESLEFFQN IPKAVTRLQT LYDVGLGYVK LGQPATTLSG
     GEAQRVKLAT ELSRRATGKT LYLIDEPTTG LSFYDVHKLL DVLQRLVDKG NSILVIEHNL
     DVIRCADWVI DLGPEGGDKG GEIIAVGTPE EVAKNPRSYT GQYLQQVLKQ YSTGRK
//
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