YIHP_ECOLI
ID YIHP_ECOLI Reviewed; 461 AA.
AC P32137; Q2M8H4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative 2,3-dihydroxypropane-1-sulfonate exporter;
GN Name=yihP; OrderedLocusNames=b3877, JW3848;
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=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP C-TERMINUS.
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 TOPOLOGY [LARGE SCALE ANALYSIS].
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).
RN [5]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=24463506; DOI=10.1038/nature12947;
RA Denger K., Weiss M., Felux A.K., Schneider A., Mayer C., Spiteller D.,
RA Huhn T., Cook A.M., Schleheck D.;
RT "Sulphoglycolysis in Escherichia coli K-12 closes a gap in the
RT biogeochemical sulphur cycle.";
RL Nature 507:114-117(2014).
CC -!- FUNCTION: Could be involved in the export of 2,3-dihydroxypropane-1-
CC sulfonate (DHPS). {ECO:0000269|PubMed:24463506}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the sodium:galactoside symporter (TC 2.A.2)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03010.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77432.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L19201; AAB03010.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76874.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77432.1; ALT_INIT; Genomic_DNA.
DR PIR; H65192; H65192.
DR RefSeq; NP_418313.4; NC_000913.3.
DR RefSeq; WP_000018380.1; NZ_SSZK01000026.1.
DR AlphaFoldDB; P32137; -.
DR SMR; P32137; -.
DR BioGRID; 4263257; 220.
DR BioGRID; 852668; 1.
DR IntAct; P32137; 2.
DR STRING; 511145.b3877; -.
DR TCDB; 2.A.2.3.9; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR PaxDb; P32137; -.
DR PRIDE; P32137; -.
DR EnsemblBacteria; AAC76874; AAC76874; b3877.
DR EnsemblBacteria; BAE77432; BAE77432; BAE77432.
DR GeneID; 948371; -.
DR KEGG; ecj:JW3848; -.
DR KEGG; eco:b3877; -.
DR PATRIC; fig|1411691.4.peg.2834; -.
DR EchoBASE; EB1788; -.
DR eggNOG; COG2211; Bacteria.
DR HOGENOM; CLU_027408_0_1_6; -.
DR InParanoid; P32137; -.
DR PhylomeDB; P32137; -.
DR BioCyc; EcoCyc:YIHP-MON; -.
DR PRO; PR:P32137; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR039672; MFS_2.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR001927; Na/Gal_symport.
DR InterPro; IPR018043; Na/Gal_symport_CS.
DR PANTHER; PTHR11328; PTHR11328; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00792; gph; 1.
DR PROSITE; PS00872; NA_GALACTOSIDE_SYMP; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..461
FT /note="Putative 2,3-dihydroxypropane-1-sulfonate exporter"
FT /id="PRO_0000170769"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..47
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..123
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..188
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..276
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..419
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 459..461
FT /note="RTA -> AHGVIIINDAAGRYKE (in Ref. 1; AAB03010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 50982 MW; BC0A9A221536967D CRC64;
MSHITTEDPA TLRLPFKEKL SYGIGDLASN ILLDIGTLYL LKFYTDVLGL PGTYGGIIFL
ISKFFTAFTD MGTGIMLDSR RKIGPKGKFR PFILYASFPV TLLAIANFVG TPFDVTGKTV
MATILFMLYG LFFSMMNCSY GAMVPAITKN PNERASLAAW RQGGATLGLL LCTVGFVPVM
NLIEGNQQLG YIFAATLFSL FGLLFMWICY SGVKERYVET QPANPAQKPG LLQSFRAIAG
NRPLFILCIA NLCTLGAFNV KLAIQVYYTQ YVLNDPILLS YMGFFSMGCI FIGVFLMPAS
VRRFGKKKVY IGGLLIWVLG DLLNYFFGGG SVSFVAFSCL AFFGSAFVNS LNWALVSDTV
EYGEWRTGVR SEGTVYTGFT FFRKVSQALA GFFPGWMLTQ IGYVPNVAQA DHTIEGLRQL
IFIYPSALAV VTIVAMGCFY SLNEKMYVRI VEEIEARKRT A
