INT2_MYCTU
ID INT2_MYCTU Reviewed; 375 AA.
AC P9WMB3; L0TD68; P71956; Q7D6T7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Putative prophage phiRv2 integrase;
GN OrderedLocusNames=Rv2659c;
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 INDUCTION BY HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
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).
CC -!- FUNCTION: Integrase is necessary for integration of the phage into the
CC host genome by site-specific recombination. In conjunction with
CC excisionase, integrase is also necessary for excision of the prophage
CC from the host genome (By similarity). {ECO:0000250}.
CC -!- INDUCTION: A possible member of the dormancy regulon. Induced in
CC response to reduced oxygen tension (hypoxia). It is hoped that this
CC regulon will give insight into the latent, or dormant phase of
CC infection. {ECO:0000269|PubMed:11416222}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45457.1; -; Genomic_DNA.
DR PIR; G70966; G70966.
DR RefSeq; NP_217175.1; NC_000962.3.
DR RefSeq; WP_003899420.1; NZ_NVQJ01000079.1.
DR AlphaFoldDB; P9WMB3; -.
DR SMR; P9WMB3; -.
DR STRING; 83332.Rv2659c; -.
DR PaxDb; P9WMB3; -.
DR DNASU; 885098; -.
DR GeneID; 885098; -.
DR KEGG; mtu:Rv2659c; -.
DR TubercuList; Rv2659c; -.
DR eggNOG; COG0582; Bacteria.
DR OMA; DVAIPPH; -.
DR PhylomeDB; P9WMB3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.10; -; 1.
DR InterPro; IPR044068; CB.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013762; Integrase-like_cat_sf.
DR InterPro; IPR002104; Integrase_catalytic.
DR InterPro; IPR010998; Integrase_recombinase_N.
DR InterPro; IPR004107; Integrase_SAM-like_N.
DR Pfam; PF14659; Phage_int_SAM_3; 1.
DR Pfam; PF00589; Phage_integrase; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 1: Evidence at protein level;
KW DNA integration; DNA recombination; DNA-binding; Reference proteome;
KW Viral genome integration; Virus entry into host cell.
FT CHAIN 1..375
FT /note="Putative prophage phiRv2 integrase"
FT /id="PRO_0000392940"
FT DOMAIN 75..153
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 175..364
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 351
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
SQ SEQUENCE 375 AA; 42176 MW; 01ED932046AC4D54 CRC64;
MTQTGKRQRR KFGRIRQFNS GRWQASYTGP DGRVYIAPKT FNAKIDAEAW LTDRRREIDR
QLWSPASGQE DRPGAPFGEY AEGWLKQRGI KDRTRAHYRK LLDNHILATF ADTDLRDITP
AAVRRWYATT AVGTPTMRAH SYSLLRAIMQ TALADDLIDS NPCRISGAST ARRVHKIRPA
TLDELETITK AMPDPYQAFV LMAAWLAMRY GELTELRRKD IDLHGEVARV RRAVVRVGEG
FKVTTPKSDA GVRDISIPPH LIPAIEDHLH KHVNPGRESL LFPSVNDPNR HLAPSALYRM
FYKARKAAGR PDLRVHDLRH SGAVLAASTG ATLAELMQRL GHSTAGAALR YQHAAKGRDR
EIAALLSKLA ENQEM