UVRA_MYCTU
ID UVRA_MYCTU Reviewed; 972 AA.
AC P9WQK7; 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 40.
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=Rv1638;
GN ORFNames=MTCY06H11.02;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND INTERACTION WITH RECA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20455546; DOI=10.1021/bi902021d;
RA Singh P., Patil K.N., Khanduja J.S., Kumar P.S., Williams A., Rossi F.,
RA Rizzi M., Davis E.O., Muniyappa K.;
RT "Mycobacterium tuberculosis UvrD1 and UvrA proteins suppress DNA strand
RT exchange promoted by cognate and noncognate RecA proteins.";
RL Biochemistry 49:4872-4883(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22467787; DOI=10.1128/jb.06654-11;
RA Houghton J., Townsend C., Williams A.R., Rodgers A., Rand L., Walker K.B.,
RA Bottger E.C., Springer B., Davis E.O.;
RT "Important role for Mycobacterium tuberculosis UvrD1 in pathogenesis and
RT persistence apart from its function in nucleotide excision repair.";
RL J. Bacteriol. 194:2916-2923(2012).
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. Alone it slightly
CC inhibits RecA-mediated DNA strand exchange, in concert with UvrD1
CC greatly inhibits RecA-mediated DNA strand exchange. {ECO:0000255|HAMAP-
CC Rule:MF_00205, ECO:0000269|PubMed:20455546,
CC ECO:0000269|PubMed:22467787}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for lesions
CC (By similarity). Interacts with RecA. {ECO:0000255|HAMAP-Rule:MF_00205,
CC ECO:0000269|PubMed:20455546}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC -!- DISRUPTION PHENOTYPE: Greatly increased sensitivity to UV light,
CC mitomycin C, slightly less sensitive to nitrosative and oxidative
CC stress; a double uvrA/uvrD1 mutant is even more sensitive. Single uvrA
CC mutant is only slightly attenuated in mouse infection, the double
CC uvrA/uvrD1 mutant is strongly attenuated at all stages of infection.
CC {ECO:0000269|PubMed:22467787}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR EMBL; AL123456; CCP44402.1; -; Genomic_DNA.
DR PIR; A70619; A70619.
DR RefSeq; NP_216154.1; NC_000962.3.
DR RefSeq; WP_003408092.1; NZ_NVQJ01000016.1.
DR PDB; 3ZQJ; X-ray; 3.40 A; A/B/C/D/E/F=1-972.
DR PDBsum; 3ZQJ; -.
DR AlphaFoldDB; P9WQK7; -.
DR SMR; P9WQK7; -.
DR STRING; 83332.Rv1638; -.
DR PaxDb; P9WQK7; -.
DR DNASU; 885685; -.
DR GeneID; 885685; -.
DR KEGG; mtu:Rv1638; -.
DR TubercuList; Rv1638; -.
DR eggNOG; COG0178; Bacteria.
DR OMA; PFEGIIP; -.
DR PhylomeDB; P9WQK7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0006974; P:cellular response to DNA damage stimulus; IEP:MTBBASE.
DR GO; GO:0060543; P:negative regulation of strand invasion; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW DNA-binding; Excision nuclease; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..972
FT /note="UvrABC system protein A"
FT /id="PRO_0000093070"
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"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 195..207
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 331..336
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 413..419
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 438..442
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 447..455
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 464..486
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 503..516
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 529..532
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 536..550
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 562..566
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 591..596
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 601..607
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 623..632
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 648..655
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 660..664
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 668..676
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 698..701
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 718..721
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 722..729
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 732..735
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 736..738
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 754..758
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 759..764
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 767..769
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 772..775
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 777..781
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 786..789
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 798..802
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 806..812
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 817..828
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 840..842
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 845..857
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 866..871
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT TURN 872..875
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 878..893
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 897..901
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 905..910
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 912..921
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT STRAND 926..932
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 934..939
FT /evidence="ECO:0007829|PDB:3ZQJ"
FT HELIX 944..950
FT /evidence="ECO:0007829|PDB:3ZQJ"
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
