NARK2_MYCTU
ID NARK2_MYCTU Reviewed; 395 AA.
AC P9WJY7; L0TAG9; P71995; Q7D820;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Probable nitrate/nitrite transporter NarK2;
GN Name=narK2; Synonyms=narK-3; OrderedLocusNames=Rv1737c;
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 INDUCTION BY HYPOXIA, ROLE IN NITRATE REDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14645286; DOI=10.1128/jb.185.24.7247-7256.2003;
RA Sohaskey C.D., Wayne L.G.;
RT "Role of narK2X and narGHJI in hypoxic upregulation of nitrate reduction by
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 185:7247-7256(2003).
RN [4]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
RN [5]
RP INDUCTION BY CARBON MONOXIDE (CO).
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA Shiloh M.U., Manzanillo P., Cox J.S.;
RT "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT macrophage infection.";
RL Cell Host Microbe 3:323-330(2008).
RN [6]
RP INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA Agarwal A., Steyn A.J.;
RT "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT tuberculosis dormancy regulon.";
RL J. Biol. Chem. 283:18032-18039(2008).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=19553548; DOI=10.1128/cvi.00111-09;
RA Black G.F., Thiel B.A., Ota M.O., Parida S.K., Adegbola R., Boom W.H.,
RA Dockrell H.M., Franken K.L., Friggen A.H., Hill P.C., Klein M.R.,
RA Lalor M.K., Mayanja H., Schoolnik G., Stanley K., Weldingh K.,
RA Kaufmann S.H., Walzl G., Ottenhoff T.H.;
RT "Immunogenicity of novel DosR regulon-encoded candidate antigens of
RT Mycobacterium tuberculosis in three high-burden populations in Africa.";
RL Clin. Vaccine Immunol. 16:1203-1212(2009).
CC -!- FUNCTION: Permits nitrate and nitrate transport into E.coli.
CC {ECO:0000269|PubMed:14645286}.
CC -!- FUNCTION: Involved in excretion of nitrite produced by the
CC dissimilatory reduction of nitrate. {ECO:0000269|PubMed:14645286}.
CC -!- ACTIVITY REGULATION: Increased nitrate reductase activity is seen under
CC hypoxic conditions, however this seems to be due to induction of the
CC probable nitrate/nitrite transporter narK2 rather than increased enzyme
CC activity of the probable nitrate reductase NarGHJI.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia), low levels of nitric oxide (NO) and
CC carbon monoxide (CO). It is hoped that this regulon will give insight
CC into the latent, or dormant phase of infection. Induction by hypoxia is
CC independent of nitrate and nitrate levels.
CC {ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:12953092,
CC ECO:0000269|PubMed:14645286, ECO:0000269|PubMed:18400743,
CC ECO:0000269|PubMed:18474359}.
CC -!- DISRUPTION PHENOTYPE: Wild-type levels of nitrite production in aerobic
CC cultures, but hypoxic cultures show no increase in nitrite production.
CC {ECO:0000269|PubMed:14645286}.
CC -!- BIOTECHNOLOGY: This protein serves as an immunogenic antigen, inducing
CC gamma-interferon responses in whole-blood cultures from M.tuberculosis-
CC exposed adults in Uganda, The Gambia and South Africa, indicating this
CC might be a good vaccine candidate. {ECO:0000269|PubMed:19553548}.
CC -!- MISCELLANEOUS: One of the activities induced in M.tuberculosis by
CC hypoxia is the dissimilatory reduction of nitrate to nitrite, which
CC serves to provide energy as the bacteria adapt to anaerobiosis.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Nitrate/nitrite porter (TC 2.A.1.8) family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44503.1; -; Genomic_DNA.
DR PIR; D70688; D70688.
DR RefSeq; NP_216253.1; NC_000962.3.
DR RefSeq; WP_003898992.1; NZ_NVQJ01000010.1.
DR AlphaFoldDB; P9WJY7; -.
DR SMR; P9WJY7; -.
DR STRING; 83332.Rv1737c; -.
DR PaxDb; P9WJY7; -.
DR GeneID; 885231; -.
DR KEGG; mtu:Rv1737c; -.
DR TubercuList; Rv1737c; -.
DR eggNOG; COG2223; Bacteria.
DR OMA; DAWWFMF; -.
DR PhylomeDB; P9WJY7; -.
DR BRENDA; 7.3.2.4; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015112; F:nitrate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0090352; P:regulation of nitrate assimilation; IMP:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
DR CDD; cd17341; MFS_NRT2_like; 1.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR044772; NO3_transporter.
DR PANTHER; PTHR23515; PTHR23515; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Nitrate assimilation; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..395
FT /note="Probable nitrate/nitrite transporter NarK2"
FT /id="PRO_0000392910"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 395 AA; 41109 MW; D901788EE33625A5 CRC64;
MRGQAANLVL ATWISVVNFW AWNLIGPLST SYARDMSLSS AEASLLVATP ILVGALGRIV
TGPLTDRFGG RAMLIAVTLA SILPVLAVGV AATMGSYALL VFFGLFLGVA GTIFAVGIPF
ANNWYQPARR GFSTGVFGMG MVGTALSAFF TPRFVRWFGL FTTHAIVAAA LASTAVVAMV
VLRDAPYFRP NADPVLPRLK AAARLPVTWE MSFLYAIVFG GFVAFSNYLP TYITTIYGFS
TVDAGARTAG FALAAVLARP VGGWLSDRIA PRHVVLASLA GTALLAFAAA LQPPPEVWSA
ATFITLAVCL GVGTGGVFAW VARRAPAASV GSVTGIVAAA GGLGGYFPPL VMGATYDPVD
NDYTVGLLLL VATALVACTY TALHAREPVS EEASR
