ID   UVRA_CHLMU              Reviewed;        1787 AA.
AC   Q9PK60;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=UvrABC system protein A;
DE            Short=UvrA protein;
DE   AltName: Full=Excinuclease ABC subunit A;
GN   Name=uvrA; OrderedLocusNames=TC_0610;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000305}.
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DR   EMBL; AE002160; AAF39441.1; -; Genomic_DNA.
DR   PIR; G81684; G81684.
DR   RefSeq; WP_010230990.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PK60; -.
DR   SMR; Q9PK60; -.
DR   STRING; 243161.TC_0610; -.
DR   PRIDE; Q9PK60; -.
DR   EnsemblBacteria; AAF39441; AAF39441; TC_0610.
DR   GeneID; 1245972; -.
DR   KEGG; cmu:TC_0610; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_3_0_0; -.
DR   OMA; SKHGWCP; -.
DR   OrthoDB; 152379at2; -.
DR   Proteomes; UP000000800; 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-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   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 5.
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; 4.
DR   TIGRFAMs; TIGR00630; uvra; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
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; Repeat; SOS response;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1787
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093042"
FT   DOMAIN          300..574
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          594..912
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          1254..1474
FT                   /note="ABC transporter 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   ZN_FING         719..742
FT                   /note="C4-type"
FT   ZN_FING         1596..1622
FT                   /note="C4-type"
FT   BINDING         410..417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         625..632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         964..971
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1509..1516
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   1787 AA;  196467 MW;  C93113B53571E06D CRC64;
     MPSIVRLSGI TVRNLKNVTV EFCPREIVLF TGVSGSGKSS LAFNTIYAAG RKRYITTLPS
     FFATRIHSLP DPAVKKVEGL SPTVAVKQNF FAQHVHATVG STTEINSYLA LLFSLDGQAY
     DPITLRPLTL YSKEKILAEI AAIPDGTQLT LLAPLPAGDI LRVRECLRQG FTKILIDGEI
     SPIHKFLATG VPVPSQLIID TLIKNASNTP RLKVSLFTTL DIGHGECCLH FDNQKRVFST
     QTTLPETQNT YTPLSPDLFS SHSHKDRCPQ CHGSGIFVSI NDPSIIQQNL SIEKNCCPFA
     GSCSILLYKT IYQSLADNLG FSLSTPWQDL SPEIQHIFLY GKEGLSLPVK LFDGTLGKTT
     QTHKQWKGVL NEIGEKIRFA NKPSRYLPKG TSYTECPRCQ KTGLSDYANA AKWHGKSFAD
     LQQMSLQELF IFLNQLPPKD PAIEEVIQGL KARLAMLIDL GLPYLSPERS VNTLSGGEQE
     RTALAKHLGA ELMGVTYVLD EPSIGLHPQD TYKLMDVIKK LRDQGNTILL VEHDEQMISL
     ADRVIDVGPG AGIFGGEVVF NGTPKEFLAN SHSLTAQYLR QEQQIPIPAK RQTSLGSITL
     SRANKHNLKN LTVSIPLGQL TVVTGVSGSG KSSLINDTLV PCVEEFIEQG SCPNLAVQGK
     LSRLVHINRD LPGRSQRSIS LTYIKAFDEL RQLFAEQPRC KPLGLTKSHF SFNTPLGACS
     ECGGLGSITA MDNQDSITCP SCSGKRFLPQ VLEIRYKNKT IADILEMTAY EAESFFLDQP
     SIHNKIQALC TLGLQYLPLG RPLYSLSGGE IQRLKLACEL SNPVKHPTLY VLDEPTTGLH
     THDVKQLIHV LQSLTDQGHS VVIIEHNMHV VKIADYVLEL GPEGGNKGGC LIASCSPEEL
     IHKHTPTSLA LRPFLSQHQE LPHLPDLRQQ PPIPAAIIIT NAHHHNLKHI DVSIPRYALT
     TVTGPSASGK HSLVFDVLHA AGNISYAELF PPYIRQALIK KTPLPSVDKV IGLSPVIAIE
     KNSAKNSSHS VASALEISDM LEELFTQIGR PYSPVSGDLL KEVSPQTIAE ELLENYAQGY
     VTITIPFPPE EDFFSYTQEM LREGFLKLYA NEQLYDLEGP FPDCLESPAL VIHHVKILEK
     NIPSILSSLS LAFSKSSSIR LHIENYGITT SKTYQLGLQD SLGNSFPSND NTTHLCPFCH
     GNGSLSTFSI LPYKNRFAEH TPLSLFTSLF PNQDPTPIYP LLEELGIPSI ALFQEMDDHS
     FQKLCLGTLQ NPGFDALCTK AMLAHPTTNF PTYLISETPC NQCQGNGTYT YEHCTRIHDI
     SLSDIYQSDV PFLKKFLLSL GKDLPLVSDI FQKLELLERV GLSQVILGQE QSSLSDGERY
     QLLLAKAFSS GLTDVIYLLE DPLAGIHPKD APSLLSVIKD LVANHNTVVV TDREGSLSKH
     ADHVIHLGPE PGPNGGYLLE TSAFRDLQPI SQSTYISDQI PKLSVSVLTS AIQIDNLSIP
     LRSLSTISGV SGSGKTTLLL EGIYKSGCAM LEKDPSLFSE IIFLDSHPQP ASSRSDISTY
     FDIAPSLRNF FSSLTQAKAL NISASMFSPN TKQGQCSDCW GLGYQLIDRA FYAMEKRSCP
     TCGGFRVQPL VQEVVYEGKH FGQLLQSSLN EVAKDFSFLK KVQKPLQTLI ANGLGYLPLG
     QNMSSLSLSE KIAIKITKYL FLPPKHPTLF LLDGVATSLD NQQKYTLLSQ LKTLVSLGHT
     VVIIENHPAF SQYADFLIQM GHKTDKTSSR IIFSGINQSP SLSNKLE