UVRA_MYCTO
ID UVRA_MYCTO Reviewed; 972 AA.
AC P9WQK6; L0T7H9; P63380; P94972;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=MT1675;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAK45944.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AE000516; AAK45944.1; ALT_INIT; Genomic_DNA.
DR PIR; A70619; A70619.
DR RefSeq; WP_003408092.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQK6; -.
DR SMR; P9WQK6; -.
DR EnsemblBacteria; AAK45944; AAK45944; MT1675.
DR KEGG; mtc:MT1675; -.
DR PATRIC; fig|83331.31.peg.1801; -.
DR HOGENOM; CLU_001370_0_2_11; -.
DR Proteomes; UP000001020; 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; 3.40.50.300; -; 3.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004602; UvrA.
DR InterPro; IPR041552; UvrA_DNA-bd.
DR InterPro; IPR041102; UvrA_inter.
DR Pfam; PF00005; ABC_tran; 1.
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; Repeat; SOS response;
KW Zinc; Zinc-finger.
FT CHAIN 1..972
FT /note="UvrABC system protein A"
FT /id="PRO_0000426759"
FT DOMAIN 315..601
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 621..950
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 257..285
FT /note="C4-type; atypical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 753..779
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 654..661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 972 AA; 106132 MW; 8937A764E592D981 CRC64;
MADRLIVKGA REHNLRSVDL DLPRDALIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSA
YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TNRNPRSTVG TITEVYDYLR LLYARAGTPH
CPTCGERVAR QTPQQIVDQV LAMPEGTRFL VLAPVVRTRK GEFADLFDKL NAQGYSRVRV
DGVVHPLTDP PKLKKQEKHD IEVVVDRLTV KAAAKRRLTD SVETALNLAD GIVVLEFVDH
ELGAPHREQR FSEKLACPNG HALAVDDLEP RSFSFNSPYG ACPECSGLGI RKEVDPELVV
PDPDRTLAQG AVAPWSNGHT AEYFTRMMAG LGEALGFDVD TPWRKLPAKA RKAILEGADE
QVHVRYRNRY GRTRSYYADF EGVLAFLQRK MSQTESEQMK ERYEGFMRDV PCPVCAGTRL
KPEILAVTLA GESKGEHGAK SIAEVCELSI ADCADFLNAL TLGPREQAIA GQVLKEIRSR
LGFLLDVGLE YLSLSRAAAT LSGGEAQRIR LATQIGSGLV GVLYVLDEPS IGLHQRDNRR
LIETLTRLRD LGNTLIVVEH DEDTIEHADW IVDIGPGAGE HGGRIVHSGP YDELLRNKDS
ITGAYLSGRE SIEIPAIRRS VDPRRQLTVV GAREHNLRGI DVSFPLGVLT SVTGVSGSGK
STLVNDILAA VLANRLNGAR QVPGRHTRVT GLDYLDKLVR VDQSPIGRTP RSNPATYTGV
FDKIRTLFAA TTEAKVRGYQ PGRFSFNVKG GRCEACTGDG TIKIEMNFLP DVYVPCEVCQ
GARYNRETLE VHYKGKTVSE VLDMSIEEAA EFFEPIAGVH RYLRTLVDVG LGYVRLGQPA
PTLSGGEAQR VKLASELQKR STGRTVYILD EPTTGLHFDD IRKLLNVING LVDKGNTVIV
IEHNLDVIKT SDWIIDLGPE GGAGGGTVVA QGTPEDVAAV PASYTGKFLA EVVGGGASAA
TSRSNRRRNV SA