UVRA_NEIMB
ID UVRA_NEIMB Reviewed; 949 AA.
AC Q9JZP1;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=NMB0962;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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. {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 -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002098; AAF41368.1; -; Genomic_DNA.
DR PIR; A81138; A81138.
DR RefSeq; NP_274000.1; NC_003112.2.
DR RefSeq; WP_002244094.1; NC_003112.2.
DR AlphaFoldDB; Q9JZP1; -.
DR SMR; Q9JZP1; -.
DR STRING; 122586.NMB0962; -.
DR PaxDb; Q9JZP1; -.
DR EnsemblBacteria; AAF41368; AAF41368; NMB0962.
DR KEGG; nme:NMB0962; -.
DR PATRIC; fig|122586.8.peg.1218; -.
DR HOGENOM; CLU_001370_0_0_4; -.
DR OMA; PFEGIIP; -.
DR Proteomes; UP000000425; 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; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..949
FT /note="UvrABC system protein A"
FT /id="PRO_0000093073"
FT DOMAIN 319..596
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 616..945
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 262..289
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 748..774
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 649..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 949 AA; 105537 MW; 153F5AE2D48CDD35 CRC64;
MCNHHPQHSH DNDTIRIRGA RTHNLKNIDL DIPRHKLVVV TGLSGSGKSS LAFDTLYAEG
QRRYVESLSA YARQFLQMMD KPDVDLIEGL SPAISIEQKS TSHNPRSTVG TVTEIHDYLR
LLYARVGTPY CPEHKLPLSS QTVSQMVDAV LKLPEDTRVM ILAPTVRERK GEFVDFFADL
QAQGFARVRV DGEVYQLDEV PKLEKNIKHN IDVVIDRVKV KADIKQRLAE SFETALRHGN
ERALAMEMDS GEEHWFSARF ACPVCSYSLP ELEPRLFSFN NPMGSCPTCD GLGNTNFFDP
EKVVAHPELS LATGAIDGWD KRNQFYFQMI QSLARHYGFD VQAAWETLPE KVKKVVLHGS
GKEVIDFTYL SERGTTFNRS HAFEGIIPNL ERRYRETDSE TVREKLREYQ NHRACPSCGG
ARLRKEARYV YVSGEPLHEV SAWPLTKTHQ FFETLDLDGN KKQIAEKILK EITERLGFLI
NVGLDYLNLS RSAETLSGGE AQRIRLASQI GSGLTGVMYV LDEPSIGLHQ RDNDRLLATL
KRLRDLGNSV IVVEHDEDAI READFVVDMG PGAGEHGGNV LIADTPENVA QCENSVTGQY
LSGKKSIAVP SERTPVNPDR MLVLKGARGN NLKNVTLELP LGLITCITGV SGSGKSTLIN
DTLAKITARE LNRAQEEPAP FDDIHGLEHL DKVINVDQSP IGRTPRSNPA TYTGLFTPIR
ELFAGVPLSR ERGYNVGRFS FNVKGGRCEA CQGDGVIKVE MHFLPDVYVP CEVCHGKRYN
RETLEIQYKG KNISQVLDMT VEEAREFFDA VPTVSRKLQT LMDVGLGYIR LGQSATTLSG
GEAQRVKLAL ELSKRDTGRT LYILDEPTTG LHFADIALLL EVIGRLKGKG NSIVIIEHNL
DVIKTADWIV DLGPEGGDGG GRIIAKGSPE QVAKVKGSYT GKYLKVVLR
