ANSP_ECOLI
ID ANSP_ECOLI Reviewed; 499 AA.
AC P77610;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=L-asparagine permease;
DE AltName: Full=L-asparagine transport protein;
GN Name=ansP; Synonyms=yncF; OrderedLocusNames=b1453, JW5234;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
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; U00096; AAC74535.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15086.2; -; Genomic_DNA.
DR RefSeq; NP_415970.4; NC_000913.3.
DR RefSeq; WP_001300590.1; NZ_SSZK01000021.1.
DR AlphaFoldDB; P77610; -.
DR SMR; P77610; -.
DR BioGRID; 4260199; 8.
DR STRING; 511145.b1453; -.
DR TCDB; 2.A.3.1.24; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P77610; -.
DR PRIDE; P77610; -.
DR EnsemblBacteria; AAC74535; AAC74535; b1453.
DR EnsemblBacteria; BAA15086; BAA15086; BAA15086.
DR GeneID; 946019; -.
DR KEGG; ecj:JW5234; -.
DR KEGG; eco:b1453; -.
DR PATRIC; fig|1411691.4.peg.815; -.
DR EchoBASE; EB3538; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_0_6; -.
DR InParanoid; P77610; -.
DR OMA; QVPYAGI; -.
DR PhylomeDB; P77610; -.
DR BioCyc; EcoCyc:ANSP-MON; -.
DR PRO; PR:P77610; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..499
FT /note="L-asparagine permease"
FT /id="PRO_0000054185"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 54233 MW; 188948BD8EC662E1 CRC64;
MSKHDTDTSD QHAAKRRWLN AHEEGYHKAM GNRQVQMIAI GGAIGTGLFL GAGARLQMAG
PALALVYLIC GLFSFFILRA LGELVLHRPS SGSFVSYARE FLGEKAAYVA GWMYFINWAM
TGIVDITAVA LYMHYWGAFG GVPQWVFALA ALTIVGTMNM IGVKWFAEME FWFALIKVLA
IVTFLVVGTV FLGSGQPLDG NTTGFHLITD NGGFFPHGLL PALVLIQGVV FAFASIEMVG
TAAGECKDPQ TMVPKAINSV IWRIGLFYVG SVVLLVMLLP WSAYQAGQSP FVTFFSKLGV
PYIGSIMNIV VLTAALSSLN SGLYCTGRIL RSMAMGGSAP SFMAKMSRQH VPYAGILATL
VVYVVGVFLN YLVPSRVFEI VLNFASLGII ASWAFIIVCQ MRLRKAIKEG KAADVSFKLP
GAPFTSWLTL LFLLSVLVLM AFDYPNGTYT IAALPIIGIL LVIGWFGVRK RVAEIHSTAP
VVEEDEEKQE IVFKPETAS
