LCTP_BACSU
ID LCTP_BACSU Reviewed; 541 AA.
AC P55910; O31470; O32395;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=L-lactate permease;
GN Name=lctP; Synonyms=ycgC; OrderedLocusNames=BSU03060;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RA Murata M., Ohki R.;
RT "Cloning and sequencing of the lct operon from Bacillus subtilis.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(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 SEQUENCE REVISION TO 262; 294; 379; 431; 520 AND 535.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP REGULATION.
RX PubMed=10809684; DOI=10.1128/jb.182.11.3072-3080.2000;
RA Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E.,
RA Dreesen O., Glaser P., Jahn D.;
RT "Fermentative metabolism of Bacillus subtilis: physiology and regulation of
RT gene expression.";
RL J. Bacteriol. 182:3072-3080(2000).
CC -!- FUNCTION: May play a role in L-lactate transport.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Strongly induced under anaerobic conditions. Activated by
CC ResDE, Fnr and ArfM.
CC -!- SIMILARITY: Belongs to the lactate permease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08940.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA21776.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D50097; BAA21776.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D50453; BAA08940.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL009126; CAB12100.2; -; Genomic_DNA.
DR PIR; F69649; F69649.
DR RefSeq; NP_388188.2; NC_000964.3.
DR RefSeq; WP_003246465.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P55910; -.
DR STRING; 224308.BSU03060; -.
DR PaxDb; P55910; -.
DR PRIDE; P55910; -.
DR EnsemblBacteria; CAB12100; CAB12100; BSU_03060.
DR GeneID; 938353; -.
DR KEGG; bsu:BSU03060; -.
DR PATRIC; fig|224308.179.peg.320; -.
DR eggNOG; COG1620; Bacteria.
DR InParanoid; P55910; -.
DR OMA; VIVLWIQ; -.
DR PhylomeDB; P55910; -.
DR BioCyc; BSUB:BSU03060-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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..541
FT /note="L-lactate permease"
FT /id="PRO_0000210373"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 262
FT /note="L -> F (in Ref. 2; BAA08940)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="K -> R (in Ref. 2; BAA08940)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="F -> V (in Ref. 2; BAA08940)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="K -> R (in Ref. 2; BAA08940)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="A -> P (in Ref. 2; BAA08940)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="I -> T (in Ref. 2; BAA08940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 57604 MW; 4BEC73739F76E3BD CRC64;
MWEQLYDPFG NEYVSALVAL TPILFFLLAL TVLKMKGILA AFLTLAVSFF VSVWAFHMPV
EKAISSVLLG IGSGLWPIGY IVLMAVWLYK IAVKTGKFTI IRSSIAGISP DQRLQLLLIG
FCFNAFLEGA AGFGVPIAIS AALLVELGFK PLKAAALCLI ANAASGAFGA IGIPVITGAQ
IGDLSALELS RTLMWTLPMI SFLIPFLLVF LLDRMKGIKQ TWPALLVVSG GYTAVQTLTM
AVLGPELANI LAALFSMGGL ALFLRKWQPK EIYREEGAGD AGEKKAYRAA DIAKAWSPFY
ILTAAITIWS LPAFKALFQE GGLLYQSTLL FKMPFLHQQI MKMPPIAPSA MPLDAVFKVD
LLSATGTAIL AAVIVTGLFS KKFSSRDAFA SLKETGKELW VPIMTICFVM GFANLANFAG
LSSSIGLALA KTGDLFPFVS PVLGWIGVFI TGSVVSNNAL FGHLQVVTGA QIGAGSDLLL
AANTAGGVMA KLVSPQSIAI AAAAVGQTGK ESKLFKRTVA YSLILLLIIC IWTFILARLG
V
