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LUTP_BACSU
ID   LUTP_BACSU              Reviewed;         563 AA.
AC   P71067;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=L-lactate permease;
GN   Name=lutP; Synonyms=yvfH; OrderedLocusNames=BSU34190;
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   Denizot F.;
RL   Submitted (APR-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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-563.
RC   STRAIN=168;
RX   PubMed=8969506; DOI=10.1099/13500872-142-11-3089;
RA   Fabret C., Quentin Y., Chapal N., Guiseppi A., Haiech J., Denizot F.;
RT   "Integrated mapping and sequencing of a 115 kb DNA fragment from Bacillus
RT   subtilis: sequence analysis of a 21 kb segment containing the sigL locus.";
RL   Microbiology 142:3089-3096(1996).
RN   [4]
RP   FUNCTION AS A LACTATE PERMEASE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=3610;
RX   PubMed=19201793; DOI=10.1128/jb.01464-08;
RA   Chai Y., Kolter R., Losick R.;
RT   "A widely conserved gene cluster required for lactate utilization in
RT   Bacillus subtilis and its involvement in biofilm formation.";
RL   J. Bacteriol. 191:2423-2430(2009).
CC   -!- FUNCTION: Is the principal permease for the uptake of L-lactate in
CC       B.subtilis. {ECO:0000269|PubMed:19201793}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are markedly impaired
CC       (but not totally blocked) in growth on L-lactate minimal medium but not
CC       impaired in growth on glucose minimal medium.
CC       {ECO:0000269|PubMed:19201793}.
CC   -!- SIMILARITY: Belongs to the lactate permease family. {ECO:0000305}.
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DR   EMBL; Z94043; CAB08002.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15424.1; -; Genomic_DNA.
DR   EMBL; Z71928; CAA96486.1; -; Genomic_DNA.
DR   PIR; A70038; A70038.
DR   RefSeq; NP_391299.1; NC_000964.3.
DR   RefSeq; WP_003228275.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; P71067; -.
DR   STRING; 224308.BSU34190; -.
DR   TCDB; 2.A.14.1.3; the lactate permease (lctp) family.
DR   PaxDb; P71067; -.
DR   PRIDE; P71067; -.
DR   EnsemblBacteria; CAB15424; CAB15424; BSU_34190.
DR   GeneID; 936322; -.
DR   KEGG; bsu:BSU34190; -.
DR   PATRIC; fig|224308.179.peg.3706; -.
DR   eggNOG; COG1620; Bacteria.
DR   InParanoid; P71067; -.
DR   OMA; LFVYKMP; -.
DR   PhylomeDB; P71067; -.
DR   BioCyc; BSUB:BSU34190-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015129; F:lactate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015295; F:solute:proton symporter activity; IBA:GO_Central.
DR   InterPro; IPR003804; Lactate_perm.
DR   PANTHER; PTHR30003; PTHR30003; 1.
DR   Pfam; PF02652; Lactate_perm; 1.
DR   TIGRFAMs; TIGR00795; lctP; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..563
FT                   /note="L-lactate permease"
FT                   /id="PRO_0000210381"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   563 AA;  59762 MW;  E3B0983059B19B08 CRC64;
     MQWTQAYTPI GGNLLLSALA ALVPIIFFFW ALAIKRMKGY TAGLATLGIA LIIAVLVYRM
     PAEKALMSAT QGAVYGLLPI GWIIVTSVFL YKITVKTGQF DIIRSSVLSI TDDRRLQALL
     IAFSFGAFLE GAAGFGAPVA ISAALLVGLG FNPLYAAGIC LIANTAPVAF GAIGIPITAV
     EGPTGIPAME ISQMVGRQLP FLSVFIPLYL IIIMSGFRKA LEIWPAILVS GVSFAVVQYL
     SSNFLGPELP DVLSALVSMA ALAVFLKWWK PKTTFRFAGE QESAASIETA RTNPAAPAYR
     GGQIFKAWSP FLLLTAMISV WGIPSVKSAL TGHYEGSAVF LKWLNAVGEK LTFSPGVPFL
     NNQIVNADGT PIEAVYKLEV LGSAGTAILI AAVLSKFITA ISWKDWGTVF KETVQELKLP
     ILTIASVVGF AYVTNSSGMS TTLGMTLALT GSMFTFFSPV LGWLGVFITG SDTSANLLFG
     NLQKVTALSV GMDPVLSVAA NSSGGVTGKM ISPQSIAVAC AAVGLAGKES DLFRFTIKHS
     LFLLLLVCII TFLQHHVFSW MIP
 
 
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