TCYK_BACSU
ID TCYK_BACSU Reviewed; 270 AA.
AC O34852;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=L-cystine-binding protein TcyK;
DE Flags: Precursor;
GN Name=tcyK; Synonyms=ytmK; OrderedLocusNames=BSU29370;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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.
RC STRAIN=168;
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 IN L-CYSTINE TRANSPORT.
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: Part of the ABC transporter complex TcyJKLMN involved in L-
CC cystine import. Is also involved in cystathionine, djenkolate, and S-
CC methylcysteine transport. {ECO:0000269|PubMed:15262924}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TcyN),
CC two transmembrane proteins (TcyL and TcyM) and two solute-binding
CC proteins (TcyJ and TcyK). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: More strongly expressed in the presence of methionine than
CC in the presence of sulfate. {ECO:0000269|PubMed:12193636}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; AF008220; AAC00326.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14897.1; -; Genomic_DNA.
DR PIR; E69996; E69996.
DR RefSeq; NP_390815.1; NC_000964.3.
DR RefSeq; WP_004399116.1; NZ_JNCM01000036.1.
DR PDB; 2O1M; X-ray; 2.00 A; A/B=22-270.
DR PDBsum; 2O1M; -.
DR AlphaFoldDB; O34852; -.
DR SMR; O34852; -.
DR STRING; 224308.BSU29370; -.
DR TCDB; 3.A.1.3.13; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34852; -.
DR PRIDE; O34852; -.
DR EnsemblBacteria; CAB14897; CAB14897; BSU_29370.
DR GeneID; 937359; -.
DR KEGG; bsu:BSU29370; -.
DR PATRIC; fig|224308.179.peg.3191; -.
DR eggNOG; COG0834; Bacteria.
DR InParanoid; O34852; -.
DR OMA; IKYQPVT; -.
DR PhylomeDB; O34852; -.
DR BioCyc; BSUB:BSU29370-MON; -.
DR SABIO-RK; O34852; -.
DR EvolutionaryTrace; O34852; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell membrane; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..270
FT /note="L-cystine-binding protein TcyK"
FT /id="PRO_0000031780"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2O1M"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:2O1M"
FT STRAND 213..229
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 234..249
FT /evidence="ECO:0007829|PDB:2O1M"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:2O1M"
SQ SEQUENCE 270 AA; 30241 MW; 6F16029F7B9C6638 CRC64;
MKTKTAFMAI LFSLITVLSA CGAGSQTTGA GQKKVQTITV GTGTQFPNIC FIDEKGDLTG
YDVELIKELD KRLPHYKFTF KTMEFSNLLV SLGQHKVDIV AHQMEKSKER EKKFLFNKVA
YNHFPLKITV LQNNDTIRGI EDLKGKRVIT SATSNGALVL KKWNEDNGRP FEIAYEGQGA
NETANQLKSG RADATISTPF AVDFQNKTST IKEKTVGNVL SNAKVYFMFN KNEQTLSDDI
DKALQEIIDD GTLKRLSLKW LGDDYSKEQY
