OPUE_BACSU
ID OPUE_BACSU Reviewed; 492 AA.
AC O06493;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Osmoregulated proline transporter OpuE {ECO:0000305};
DE AltName: Full=Osmoprotectant uptake {ECO:0000303|PubMed:11902719};
DE AltName: Full=Proline uptake system {ECO:0000303|PubMed:11902719};
GN Name=opuE {ECO:0000303|PubMed:11902719}; Synonyms=yerK;
GN OrderedLocusNames=BSU06660;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=11902719; DOI=10.1046/j.1365-2958.1997.4441809.x;
RA von Blohn C., Kempf B., Kappes R.M., Bremer E.;
RT "Osmostress response in Bacillus subtilis: characterization of a proline
RT uptake system (OpuE) regulated by high osmolarity and the alternative
RT transcription factor sigma B.";
RL Mol. Microbiol. 25:175-187(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA Borriss R., Porwollik S., Schroeter R.;
RT "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT region devoted to purine uptake and metabolism, and containing the genes
RT cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT sequence.";
RL Microbiology 142:3027-3031(1996).
RN [3]
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 [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168 / JH642;
RX PubMed=22139509; DOI=10.1128/jb.06380-11;
RA Moses S., Sinner T., Zaprasis A., Stoeveken N., Hoffmann T., Belitsky B.R.,
RA Sonenshein A.L., Bremer E.;
RT "Proline utilization by Bacillus subtilis: uptake and catabolism.";
RL J. Bacteriol. 194:745-758(2012).
CC -!- FUNCTION: Catalyzes the uptake of extracellular proline under high-
CC osmolarity growth conditions. Essential for the use of proline present
CC in the environment as an osmoprotectant. {ECO:0000269|PubMed:11902719,
CC ECO:0000269|PubMed:22139509}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out);
CC Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039;
CC Evidence={ECO:0000305|PubMed:11902719, ECO:0000305|PubMed:22139509};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for proline {ECO:0000269|PubMed:22139509};
CC Vmax=27 nmol/min/mg enzyme {ECO:0000269|PubMed:22139509};
CC Vmax=19 nmol/min/mg enzyme (in the presence of 1 mM proline)
CC {ECO:0000269|PubMed:22139509};
CC Vmax=104 nmol/min/mg enzyme (in the presence of 0.4 M NaCl)
CC {ECO:0000269|PubMed:22139509};
CC Vmax=252 nmol/min/mg enzyme (in the presence of 0.6 M NaCl)
CC {ECO:0000269|PubMed:22139509};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Induced under high-osmolarity growth conditions. Has two
CC osmoregulated and tightly spaced promoters. The first promoter is sigma
CC A-dependent and the second promoter is controlled by the general stress
CC transcription factor sigma B. {ECO:0000269|PubMed:11902719}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene eliminates the osmotically
CC stimulated proline transport activity and practically abolishes the
CC ability to use proline as an osmoprotectant.
CC {ECO:0000269|PubMed:11902719}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; U92466; AAB66512.1; -; Genomic_DNA.
DR EMBL; AF011545; AAB72182.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12486.1; -; Genomic_DNA.
DR PIR; H69670; H69670.
DR RefSeq; NP_388548.1; NC_000964.3.
DR RefSeq; WP_003242814.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O06493; -.
DR SMR; O06493; -.
DR STRING; 224308.BSU06660; -.
DR PaxDb; O06493; -.
DR PRIDE; O06493; -.
DR EnsemblBacteria; CAB12486; CAB12486; BSU_06660.
DR GeneID; 939439; -.
DR KEGG; bsu:BSU06660; -.
DR PATRIC; fig|224308.179.peg.724; -.
DR eggNOG; COG0591; Bacteria.
DR InParanoid; O06493; -.
DR OMA; AWKTKNT; -.
DR PhylomeDB; O06493; -.
DR BioCyc; BSUB:BSU06660-MON; -.
DR SABIO-RK; O06493; -.
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:0005298; F:proline:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0031402; F:sodium ion binding; IEA:InterPro.
DR GO; GO:0015824; P:proline transport; IEA:InterPro.
DR CDD; cd11475; SLC5sbd_PutP; 1.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR011851; Na/Pro_symporter.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR018212; Na/solute_symporter_CS.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR02121; Na_Pro_sym; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..492
FT /note="Osmoregulated proline transporter OpuE"
FT /id="PRO_0000105404"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 492 AA; 53283 MW; 23459873F1E799E6 CRC64;
MSIEIIISLG IYFIAMLLIG WYAFKKTTDI NDYMLGGRGL GPFVTALSAG AADMSGWMLM
GVPGAMFATG LSTLWLALGL TIGAYSNYLL LAPRLRAYTE AADDAITIPD FFDKRFQHSS
SLLKIVSALI IMIFFTLYTS SGMVSGGRLF ESAFGADYKL GLFLTTAVVV LYTLFGGFLA
VSLTDFVQGA IMFAALVLVP IVAFTHVGGV APTFHEIDAV NPHLLDIFKG ASVISIISYL
AWGLGYYGQP HIIVRFMAIK DIKDLKPARR IGMSWMIITV LGSVLTGLIG VAYAHKFGVA
VKDPEMIFII FSKILFHPLI TGFLLSAILA AIMSSISSQL LVTASAVTED LYRSFFRRKA
SDKELVMIGR LSVLVIAVIA VLLSLNPNST ILDLVGYAWA GFGSAFGPAI LLSLYWKRMN
EWGALAAMIV GAATVLIWIT TGLAKSTGVY EIIPGFILSM IAGIIVSMIT KRPAKASYRL
FGVMEKLLKR KK
