ANSP2_MYCTU
ID ANSP2_MYCTU Reviewed; 487 AA.
AC P9WQM7; L0T3E0; O06297; P0A4W0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=L-asparagine permease 2;
DE AltName: Full=L-asparagine transport protein 2;
GN Name=ansP2 {ECO:0000303|PubMed:24586151}; OrderedLocusNames=Rv0346c;
GN ORFNames=MTCY13E10.06c;
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 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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24586151; DOI=10.1371/journal.ppat.1003928;
RA Gouzy A., Larrouy-Maumus G., Bottai D., Levillain F., Dumas A.,
RA Wallach J.B., Caire-Brandli I., de Chastellier C., Wu T.D., Poincloux R.,
RA Brosch R., Guerquin-Kern J.L., Schnappinger D., Sorio de Carvalho L.P.,
RA Poquet Y., Neyrolles O.;
RT "Mycobacterium tuberculosis exploits asparagine to assimilate nitrogen and
RT resist acid stress during infection.";
RL PLoS Pathog. 10:e1003928-e1003928(2014).
CC -!- FUNCTION: Dual function in both nitrogen assimilation and in protection
CC against acid stress during infection (PubMed:24586151). Involved in
CC asparagine uptake (PubMed:24586151). {ECO:0000269|PubMed:24586151}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Asparagine transport is partially impaired in the
CC mutant. Knockout mutant is impaired in nitrogen incorporation from
CC asparagine into other amino acids, such as glutamate and glutamine.
CC Growth of the knockout strain is greatly reduced at pH 5.5 in the
CC presence of asparagine as sole nitrogen source. Mutant is not
CC attenuated in immune-competent mice. {ECO:0000269|PubMed:24586151}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43076.1; -; Genomic_DNA.
DR PIR; C70574; C70574.
DR RefSeq; WP_003898409.1; NZ_NVQJ01000002.1.
DR RefSeq; YP_177718.1; NC_000962.3.
DR AlphaFoldDB; P9WQM7; -.
DR SMR; P9WQM7; -.
DR STRING; 83332.Rv0346c; -.
DR PaxDb; P9WQM7; -.
DR DNASU; 886530; -.
DR GeneID; 886530; -.
DR KEGG; mtu:Rv0346c; -.
DR TubercuList; Rv0346c; -.
DR eggNOG; COG1113; Bacteria.
DR OMA; LMIPGIQ; -.
DR PhylomeDB; P9WQM7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..487
FT /note="L-asparagine permease 2"
FT /id="PRO_0000054190"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 487 AA; 52195 MW; 3572502DB6ACD987 CRC64;
MPPLDITDER LTREDTGYHK GLHSRQLQMI ALGGAIGTGL FLGAGGRLAS AGPGLFLVYG
ICGIFVFLIL RALGELVLHR PSSGSFVSYA REFYGEKVAF VAGWMYFLNW AMTGIVDTTA
IAHYCHYWRA FQPIPQWTLA LIALLVVLSM NLISVRLFGE LEFWASLIKV IALVTFLIVG
TVFLAGRYKI DGQETGVSLW SSHGGIVPTG LLPIVLVTSG VVFAYAAIEL VGIAAGETAE
PAKIMPRAIN SVVLRIACFY VGSTVLLALL LPYTAYKEHV SPFVTFFSKI GIDAAGSVMN
LVVLTAALSS LNAGLYSTGR ILRSMAINGS GPRFTAPMSK TGVPYGGILL TAGIGLLGII
LNAIKPSQAF EIVLHIAATG VIAAWATIVA CQLRLHRMAN AGQLQRPKFR MPLSPFSGYL
TLAFLAGVLI LMYFDEQHGP WMIAATVIGV PALIGGWYLV RNRVTAVAHH AIDHTKSVAV
VHSADPI
