ID   UVRA_CHLTR              Reviewed;        1786 AA.
AC   O84337;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=UvrABC system protein A;
DE            Short=UvrA protein;
DE   AltName: Full=Excinuclease ABC subunit A;
GN   Name=uvrA; OrderedLocusNames=CT_333;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC67928.1; -; Genomic_DNA.
DR   PIR; H71527; H71527.
DR   RefSeq; NP_219840.1; NC_000117.1.
DR   RefSeq; WP_010725161.1; NC_000117.1.
DR   AlphaFoldDB; O84337; -.
DR   SMR; O84337; -.
DR   STRING; 813.O172_01815; -.
DR   EnsemblBacteria; AAC67928; AAC67928; CT_333.
DR   GeneID; 884785; -.
DR   KEGG; ctr:CT_333; -.
DR   PATRIC; fig|272561.5.peg.359; -.
DR   HOGENOM; CLU_001370_3_1_0; -.
DR   InParanoid; O84337; -.
DR   OMA; SKHGWCP; -.
DR   Proteomes; UP000000431; 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; -; 2.
DR   Gene3D; 3.40.50.300; -; 5.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
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; PS50893; ABC_TRANSPORTER_2; 2.
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; SOS response; Zinc; Zinc-finger.
FT   CHAIN           1..1786
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093044"
FT   DOMAIN          314..580
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          590..913
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   ZN_FING         719..742
FT                   /note="C4-type"
FT   ZN_FING         1602..1628
FT                   /note="C4-type"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1516..1523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   1786 AA;  196949 MW;  02D6862EE15DE070 CRC64;
     MSSIVRLSGI TVRNLKNITV EFCPREIVLF TGVSGSGKSS LAFNTIYAAG RKRYLATLPS
     FFATKLDSLP DPSVKKIEGL SPTVAVKQNF FEQHIHATVG STTEINSYLA LLFSLEGQAY
     DPVTLHPLTL YSKEKILSEI AAIPDGTQLT LLAPLPARDV LTVRECLRQG FTKVLIDEEV
     VPIHKFLTTG IPVPGQLIVD TLIKNTSNTP RLKVSLFTTL DIGHGECSLH FDNQKRVFST
     QATLPETQQT YAPLSPDLFS SHSHKDRCPQ CQGSGIFISI DDPCIIQQTL SIEDNCCPFA
     GNCSTFLYRT IYQSLADSLG FSLSTPWQNL SPEIQHIFLY GKEGLSIPVK LFDGTLGKKT
     QTHKQWKGVL NEIGEKIRFS NKPARYLPKG TSYTVCPRCN KTGLSDYANA TRWHGKSFAD
     FQQMSLQELF IFLNQLPEKE LAIEEVIQGF KSRLTILIDL GLPYLSPERA IDTLSGGERE
     RTALAKHLGA ELIGVMYILD EPSIGLHPQD THKLMNVIRR LRDQGNTVLL VEHDEQMISL
     ADRVIDIGPG AGIFGGEVVF NGSPREFLAK SDSLTAQYLR QEQHISVPAK RTNSLGTITL
     SKANKHNLKD LTVSIPLGQM TVVTGVSGSG KSSLINDTLV PCVEEFIEQG FCSTLSIQGA
     LSRLVHINRD LPGRSQRSIP LTYIKAFDEV RQLFAEQPRC KTLGLTKSHF SFNTPLGACA
     ECGGLGSITT TDNRDSITCP SCLGKRFLPQ VLEVRYKNKT IADILEMTAY EAKNFFLDEP
     SIHQKIETLC TLGLQYLPLG RPLYSLSGGE IQRLKLAYEL LAPVKHPTLY VLDEPTTGLH
     THDVKQLIYV VQSLIHQGHS VIIIEHNMHV VKVADYILEL GPEGGNKGGY LIASCSPEEL
     IHKHTPTAIA LRPFLSSPQE LPYLPDPSPK PPVPAAITIA NAHQHNLKHI DLSIPRYALT
     AVTGPSASGK HSLVFDILHA AGNIAYAELF PPYIRQALIK KTPLPAVDKV TGLSPVIAIE
     KTSASRNSNH SVASALEISE MLESLFTRIG HPYSPISGDT LRTISPETIA EELLTHYTKG
     YVTITVPFPK EEEFFSYTQE MLQEGFLKLY ANEQFYDLDG PFPTSLENPA LVIHHVKILE
     KNLPSLLASL TLAFSKASSV CLHIEYAGTS LSKTYRQGLQ DASGNLFPNI ETPSILNHES
     YLCPLCHGKG FLSTCSILPH KKRFAQHTPI SLFTSLFPNQ DPSPIYPLLN ELGIPSIALF
     QEIDILSFES LCLGTQQHLG LNALCTKAML MESEEDFPPD LISKTPCNQC QGLGVYTYKH
     CTRIHSISLS EIYQSNVAFL KKLLLSVEEE PSLVQDILSR LDLLDRVGLG YVILGQEQQS
     LSDGEHYRLL LAKAFSSGLT DVIYLLEDPL AGIHPEDAPC LLAVIKKLVT NHNTVIVTDR
     EGSLAEHADY LLHLGPEPGP NGGYLLSTSA LKQSQPVLCN TRSSEETPQL SVSVSTSTIQ
     IENLAFPLQR LSTISGVSGS GKTTLLNSIY EHGCAILEKD PSVFSEIIFL DSYPQIASSR
     SDISTYFDIA PSLRNFYASL TQAKALNISV SMFSPNTKQG QCSDCWGLGY QWIDRAFYAM
     EKRPCPTCGG FRVQPLIQEV VYEGKHFGQL LQASLNEVAE TFSFLKKIQK PLHTLITNDL
     GYLSLGQNMA SLSLSEKIAI KLTKHLFLPP KHPTLFLLDE IATSLDNQQQ SALLVQLNTL
     VSLGHTVVII ENHPAFSQQA DFWIQMGRKT DNHILFAGPN PNLSFT