ID   UVRA_SYNY3              Reviewed;         970 AA.
AC   P73412;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205};
DE            Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; OrderedLocusNames=slr1844;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   DISCUSSION OF SOS REGULON.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=15225304; DOI=10.1111/j.1365-2958.2004.04100.x;
RA   Domain F., Houot L., Chauvat F., Cassier-Chauvat C.;
RT   "Function and regulation of the cyanobacterial genes lexA, recA and ruvB:
RT   LexA is critical to the survival of cells facing inorganic carbon
RT   starvation.";
RL   Mol. Microbiol. 53:65-80(2004).
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:0000255|HAMAP-
CC       Rule:MF_00205}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000255|HAMAP-Rule:MF_00205}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC   -!- MISCELLANEOUS: This bacterium is considerably more resistant to UV and
CC       gamma irradiation than E.coli; the E.coli-like SOS regulon model is not
CC       an appropriate model for DNA repair in this cyanobacterium.
CC       {ECO:0000305|PubMed:15225304}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR   EMBL; BA000022; BAA17452.1; -; Genomic_DNA.
DR   PIR; S77349; S77349.
DR   AlphaFoldDB; P73412; -.
DR   SMR; P73412; -.
DR   IntAct; P73412; 2.
DR   STRING; 1148.1652531; -.
DR   PaxDb; P73412; -.
DR   PRIDE; P73412; -.
DR   EnsemblBacteria; BAA17452; BAA17452; BAA17452.
DR   KEGG; syn:slr1844; -.
DR   eggNOG; COG0178; Bacteria.
DR   InParanoid; P73412; -.
DR   OMA; PFEGIIP; -.
DR   PhylomeDB; P73412; -.
DR   Proteomes; UP000001425; 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   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00630; uvra; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW   Excision nuclease; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..970
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093106"
FT   DOMAIN          340..617
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          637..965
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         284..311
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         768..794
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         669..676
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   970 AA;  107482 MW;  BBC4948B76967E64 CRC64;
     MPEQNSIRIR GARQHNLKNV NLDLPRDRLI VFTGVSGSGK SSLAFDTIFA EGQRRYVESL
     SAYARQFLGQ LDKPDVDSIE GLSPAISIDQ KSTSHNPRST VGTVTEIYDY LRLLFGRAGS
     PHCPHCQRNI APQTIDQMCD RVMELPDRTK FQILAPVVKG KKGTHVQLLS SLVSQGFVRV
     RINGEVRELS DNIELKKNQA HTIEIVIDRL IKKEGLQERL VDSLSTCLKQ AEGTAIIDIL
     DKPTLAVLDG GKKDDKEALK AAENGQAYHA ELPKEIIFSE NFACPEHGAV MDELSPRLFS
     FNSPYGACPD CHGIGFVRSF CPDLVIPDPE KPVYVAIAPW SEKDNSYYLS LLYSLGQHFD
     FQLQTPWKKL TKEQKEIILY GTEEEIWFEG ESRYRNKQGY YRRFAGALNI LQKNYDETNS
     DAIKQKLEKY IINQPCHTCG GKRLKPEALA VKLGQYNINN LTSVPIRQTL ERIENLELTS
     RQAMIGELAL KEIKARLQFL LDVGLDYLTL DRAAMTLSGG EAQRIRLATQ IGSGLTGVLY
     VLDEPSIGLH QRDNNRLLAT LTKLRDLGNT LIVVEHDEDT IRHADYIVDI GPKAGIHGGE
     IVCQGDFQTL LKNQRSLTGA YLSGREAIAT PEERRNGNGA KLTLQGCCHN NLRNIDVTIP
     LGKLVCVTGV SGSGKSTLVN ELLHPALQHY LSRQVAFPKN LGEITGLQAI DKVIVIDQSP
     IGRTPRSNPA TYTGIFDSIR EIFTQTIEAK ARGYKPGQFS FNVKGGRCEA CAGQGVNVIE
     MNFLPDVYVQ CDVCKGARYN RETLQVKYKG HSIADVLAMT TEEALTVFEN IPRAVNRLQT
     LVDVGLGYIK LGQPAPTLSG GEAQRVKLAS ELSRRATGKT LYLIDEPTTG LSFYDVHHLL
     NVLQRLVDKG NSVLVIEHNL DVIRCSDWII DLGPEGGDRG GKIMVAGTPE TVAQHPSSYT
     GKYLAKVLQS