YIAN_ECOLI
ID YIAN_ECOLI Reviewed; 425 AA.
AC P37675; Q2M7P1; Q6BF20;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN;
GN Name=yiaN; OrderedLocusNames=b3578, JW5651;
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 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
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 [5]
RP PRELIMINARY FUNCTION.
RC STRAIN=K12;
RX PubMed=14668138; DOI=10.1080/09687680310001607369;
RA Plantinga T.H., van der Does C., Badia J., Aguilar J., Konings W.N.,
RA Driessen A.J.M.;
RT "Functional characterization of the Escherichia coli K-12 yiaMNO transport
RT protein genes.";
RL Mol. Membr. Biol. 21:51-57(2004).
RN [6]
RP DELETION STUDIES.
RC STRAIN=K12;
RX PubMed=15870475; DOI=10.1099/mic.0.27851-0;
RA Plantinga T.H., van der Does C., Tomkiewicz D., van Keulen G.,
RA Konings W.N., Driessen A.J.M.;
RT "Deletion of the yiaMNO transporter genes affects the growth
RT characteristics of Escherichia coli K-12.";
RL Microbiology 151:1683-1689(2005).
RN [7]
RP FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16385129; DOI=10.1099/mic.0.28334-0;
RA Thomas G.H., Southworth T., Leon-Kempis M.R., Leech A., Kelly D.J.;
RT "Novel ligands for the extracellular solute receptors of two bacterial TRAP
RT transporters.";
RL Microbiology 152:187-198(2006).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system YiaMNO involved in the uptake of 2,3-diketo-L-
CC gulonate. {ECO:0000269|PubMed:16385129}.
CC -!- SUBUNIT: The complex comprises the extracytoplasmic solute receptor
CC protein YiaO, and the two transmembrane proteins YiaM and YiaN.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAP transporter large permease family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally proposed to be a subunit from an L-xylulose
CC uptake system, but PubMed:16385129 shows that it does not bind L- or D-
CC xylulose. {ECO:0000305|PubMed:14668138}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18555.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18555.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48194.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77715.1; -; Genomic_DNA.
DR PIR; S47799; S47799.
DR RefSeq; WP_000279599.1; NZ_SSZK01000041.1.
DR RefSeq; YP_026232.1; NC_000913.3.
DR AlphaFoldDB; P37675; -.
DR BioGRID; 4262549; 11.
DR ComplexPortal; CPX-4681; YiaMNO tripartite ATP-independent periplasmic transporter complex.
DR STRING; 511145.b3578; -.
DR TCDB; 2.A.56.1.2; the tripartite atp-independent periplasmic transporter (trap-t) family.
DR PaxDb; P37675; -.
DR PRIDE; P37675; -.
DR EnsemblBacteria; AAT48194; AAT48194; b3578.
DR EnsemblBacteria; BAE77715; BAE77715; BAE77715.
DR GeneID; 66672533; -.
DR GeneID; 948092; -.
DR KEGG; ecj:JW5651; -.
DR KEGG; eco:b3578; -.
DR PATRIC; fig|1411691.4.peg.3134; -.
DR EchoBASE; EB2190; -.
DR eggNOG; COG1593; Bacteria.
DR HOGENOM; CLU_019824_4_1_6; -.
DR InParanoid; P37675; -.
DR OMA; LPGWING; -.
DR PhylomeDB; P37675; -.
DR BioCyc; EcoCyc:EG12282-MON; -.
DR BioCyc; MetaCyc:EG12282-MON; -.
DR PRO; PR:P37675; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0031317; C:tripartite ATP-independent periplasmic transporter complex; IC:ComplexPortal.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0034219; P:carbohydrate transmembrane transport; IDA:EcoCyc.
DR GO; GO:1902075; P:cellular response to salt; IC:ComplexPortal.
DR GO; GO:1900190; P:regulation of single-species biofilm formation; IC:ComplexPortal.
DR InterPro; IPR010656; DctM.
DR InterPro; IPR004681; TRAP_DctM.
DR PANTHER; PTHR33362; PTHR33362; 1.
DR Pfam; PF06808; DctM; 1.
DR PIRSF; PIRSF006066; HI0050; 1.
DR TIGRFAMs; TIGR00786; dctM; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..425
FT /note="2,3-diketo-L-gulonate TRAP transporter large
FT permease protein YiaN"
FT /id="PRO_0000169598"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 425 AA; 45368 MW; 4A90B9E035B1C98A CRC64;
MAVLIFLGCL LGGIAIGLPI AWALLLCGAA LMFWLDMFDV QIMAQTLVNG ADSFSLLAIP
FFVLAGEIMN AGGLSKRIVD LPMKLVGHKP GGLGYVGVLA AMIMASLSGS AVADTAAVAA
LLVPMMRSAN YPVNRAAGLI ASGGIIAPII PPSIPFIIFG VSSGLSISKL FMAGIAPGMM
MGATLMLTWW WQASRLNLPR QQKATMQEIW HSFVSGIWAL FLPVIIIGGF RSGLFTPTEA
GAVAAFYALF VATVIYREMT FATLWHVLIG AAKTTSVVMF LVASAQVSAW LITIAELPMM
VSDLLQPLVD SPRLLFIVIM VAILIVGMVM DLTPTVLILT PVLMPLVKEA GIDPIYFGVM
FIINCSIGLI TPPIGNVLNV ISGVAKLKFD DAVRGVFPYV LVLYSLLVVF VFIPDLIILP
LKWIN
