TCYP_BACSU
ID TCYP_BACSU Reviewed; 463 AA.
AC P54596;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=L-cystine uptake protein TcyP;
DE AltName: Full=Symporter YhcL;
DE AltName: Full=Transporter of cystine TcyP;
GN Name=tcyP; Synonyms=yhcL; OrderedLocusNames=BSU09130;
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;
RX PubMed=8969498; DOI=10.1099/13500872-142-11-3021;
RA Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RT "A 22 kb DNA sequence in the cspB-glpPFKD region at 75 degrees on the
RT Bacillus subtilis chromosome.";
RL Microbiology 142:3021-3026(1996).
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 INDUCTION.
RX PubMed=12193636; DOI=10.1128/jb.184.18.5179-5186.2002;
RA Auger S., Danchin A., Martin-Verstraete I.;
RT "Global expression profile of Bacillus subtilis grown in the presence of
RT sulfate or methionine.";
RL J. Bacteriol. 184:5179-5186(2002).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168;
RX PubMed=15262924; DOI=10.1128/jb.186.15.4875-4884.2004;
RA Burguiere P., Auger S., Hullo M.-F., Danchin A., Martin-Verstraete I.;
RT "Three different systems participate in L-cystine uptake in Bacillus
RT subtilis.";
RL J. Bacteriol. 186:4875-4884(2004).
CC -!- FUNCTION: Mediates uptake of L-cystine, the oxidized form of L-
CC cysteine. Although it is more specific for L-cystine, it could also
CC transport a much broader range of amino acids and sulfur compounds
CC including S-methylcysteine. {ECO:0000269|PubMed:15262924}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for L-cystine {ECO:0000269|PubMed:15262924};
CC Vmax=1.9 nmol/min/mg enzyme for the wild-type
CC {ECO:0000269|PubMed:15262924};
CC Vmax=0.85 nmol/min/mg enzyme for tcyP deletion mutant
CC {ECO:0000269|PubMed:15262924};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: More strongly expressed in the presence of methionine than
CC in presence of sulfate. Strongly inhibited by seleno-DL-cystine.
CC {ECO:0000269|PubMed:12193636}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR EMBL; X96983; CAA65696.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12741.1; -; Genomic_DNA.
DR PIR; H69822; H69822.
DR RefSeq; NP_388794.1; NC_000964.3.
DR RefSeq; WP_003244685.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P54596; -.
DR SMR; P54596; -.
DR STRING; 224308.BSU09130; -.
DR TCDB; 2.A.23.1.4; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR PaxDb; P54596; -.
DR EnsemblBacteria; CAB12741; CAB12741; BSU_09130.
DR GeneID; 939257; -.
DR KEGG; bsu:BSU09130; -.
DR PATRIC; fig|224308.179.peg.987; -.
DR eggNOG; COG1823; Bacteria.
DR InParanoid; P54596; -.
DR OMA; YFCTTII; -.
DR PhylomeDB; P54596; -.
DR BioCyc; BSUB:BSU09130-MON; -.
DR SABIO-RK; P54596; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR Gene3D; 1.10.3860.10; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..463
FT /note="L-cystine uptake protein TcyP"
FT /id="PRO_0000202123"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 48982 MW; FA69EEAF5EC45F89 CRC64;
METLLVVLHV FILFLLILGL FVMQKKHVSF SKRVFTALGL GIVFGFALQL IYGPTSNIVI
QTADWFNIAG GGYVKLLQMV VMPLVFISIL GAFTKLKLTK NLGKISGLII GILVATTAVA
AAVGIASALS FDLQAIQVDQ GSTELSRGQE LQQKSEDMTA KTLPQQIVEL LPGNPFLDFT
GARPTSTIAV VIFAAFLGVA FLGVKHKQPE QAETFKKLVD AVYAIVMRVV TLILRLTPYG
VLAIMTKTIA TSDLDSILKL GMFVIASYAA LITMFIIHLL LLTFSGLNPV IYLKKAVPVL
VFAFTSRSSA GALPLNIKTQ RSMGVPEGIA NFAGSFGLSI GQNGCAGIYP AMLAMMIAPT
VGQNPFDPVF IITVIAVVAI SSFGVAGVGG GATFAALLVL SSLNMPVALA GLLISIEPLI
DMGRTALNVS GSMTSGLITS KVTKEIDQGA FHDQSRVIEA EEA
