STET_BACSU
ID STET_BACSU Reviewed; 438 AA.
AC O34739; Q7B3R0;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serine/threonine exchanger SteT;
GN Name=steT; Synonyms=ykbA; OrderedLocusNames=BSU12860;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION AS A TRANSPORTER, SUBUNIT, AND MUTAGENESIS OF CYS-94; CYS-141;
RP CYS-168; CYS-291 AND CYS-415.
RX PubMed=17344220; DOI=10.1074/jbc.m610695200;
RA Reig N., del Rio C., Casagrande F., Ratera M., Gelpi J.L., Torrents D.,
RA Henderson P.J.F., Xie H., Baldwin S.A., Zorzano A., Fotiadis D.,
RA Palacin M.;
RT "Functional and structural characterization of the first prokaryotic member
RT of the L-amino acid transporter (LAT) family: a model for APC
RT transporters.";
RL J. Biol. Chem. 282:13270-13281(2007).
CC -!- FUNCTION: Exhibits an obligate exchange activity for serine, threonine
CC and aromatic amino acids. {ECO:0000269|PubMed:17344220}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17344220}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
CC {ECO:0000305}.
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DR EMBL; AJ002571; CAA05566.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13143.1; -; Genomic_DNA.
DR PIR; B69855; B69855.
DR RefSeq; NP_389169.1; NC_000964.3.
DR RefSeq; WP_003244819.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34739; -.
DR SMR; O34739; -.
DR STRING; 224308.BSU12860; -.
DR TCDB; 2.A.3.8.12; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; O34739; -.
DR EnsemblBacteria; CAB13143; CAB13143; BSU_12860.
DR GeneID; 936518; -.
DR KEGG; bsu:BSU12860; -.
DR PATRIC; fig|224308.179.peg.1395; -.
DR eggNOG; COG0531; Bacteria.
DR InParanoid; O34739; -.
DR OMA; YDGWILI; -.
DR PhylomeDB; O34739; -.
DR BioCyc; BSUB:BSU12860-MON; -.
DR Proteomes; UP000001570; 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:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..438
FT /note="Serine/threonine exchanger SteT"
FT /id="PRO_0000376828"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 94
FT /note="C->S: Retains 25% of the transport activity; when
FT associated with S-141; S-168; S-291 and S-415."
FT /evidence="ECO:0000269|PubMed:17344220"
FT MUTAGEN 141
FT /note="C->S: Retains 25% of the transport activity; when
FT associated with S-94; S-168; S-291 and S-415."
FT /evidence="ECO:0000269|PubMed:17344220"
FT MUTAGEN 168
FT /note="C->S: Retains 25% of the transport activity; when
FT associated with S-94; S-141; S-291 and S-415."
FT /evidence="ECO:0000269|PubMed:17344220"
FT MUTAGEN 291
FT /note="C->S: Retains 25% of the transport activity; when
FT associated with S-94; S-141; S-168 and S-415."
FT /evidence="ECO:0000269|PubMed:17344220"
FT MUTAGEN 415
FT /note="C->S: Retains 25% of the transport activity; when
FT associated with S-94; S-141; S-168 and S-291."
FT /evidence="ECO:0000269|PubMed:17344220"
SQ SEQUENCE 438 AA; 47148 MW; EB67441F8A1D79D7 CRC64;
MHTEDNGLKK EIGLLFALTL VIGTIIGSGV FMKPGAVLAY SGDSKMALFA WLLGGILTLA
GGLTIAEIGT QIPKTGGLYT YLEEVYGEFW GFLCGWVQII IYGPAIIGAL GLYFGSLMAN
LFGWGSGLSK VIGIIAVLFL CVINIIGTKY GGFVQTLTTI GKLIPIACII VFGLWKGDQH
IFTAVNESIS DMNFGAAILA TLFAYDGWIL LAALGGEMKN PEKLLPRAMT GGLLIVTAIY
IFINFALLHI LSANEIVTLG ENATSTAATM LFGSIGGKLI SVGIIVSIFG CLNGKVLSFP
RVSFAMAERK QLPFAEKLSH VHPSFRTPWI AISFQIALAL IMMLISNPDK LSEISIFMIY
IFYVMAFFAV FILRKRAKGE KRAYSVPLYP FMPILAIAGS FFVLGSTLIT DTMSCGLSIL
IGLAGLPVYY GMKKRKAS
