ID   TCYN_BACSU              Reviewed;         259 AA.
AC   O34900;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=L-cystine import ATP-binding protein TcyN;
DE            EC=7.4.2.-;
GN   Name=tcyN; Synonyms=ytmN; OrderedLocusNames=BSU29340;
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. Responsible for energy coupling to the transport system
CC       (Probable). Is also involved in cystathionine, djenkolate, and S-
CC       methylcysteine transport. {ECO:0000269|PubMed:15262924, ECO:0000305}.
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:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
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 ABC transporter superfamily. L-cystine
CC       importer (TC 3.A.1.3.13) family. {ECO:0000305}.
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DR   EMBL; AF008220; AAC00329.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14894.1; -; Genomic_DNA.
DR   PIR; F69641; F69641.
DR   RefSeq; NP_390812.1; NC_000964.3.
DR   RefSeq; WP_004398701.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34900; -.
DR   SMR; O34900; -.
DR   STRING; 224308.BSU29340; -.
DR   TCDB; 3.A.1.3.13; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O34900; -.
DR   PRIDE; O34900; -.
DR   EnsemblBacteria; CAB14894; CAB14894; BSU_29340.
DR   GeneID; 937364; -.
DR   KEGG; bsu:BSU29340; -.
DR   PATRIC; fig|224308.179.peg.3188; -.
DR   eggNOG; COG1126; Bacteria.
DR   InParanoid; O34900; -.
DR   OMA; VLATHEM; -.
DR   PhylomeDB; O34900; -.
DR   BioCyc; BSUB:BSU29340-MON; -.
DR   SABIO-RK; O34900; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015424; F:ABC-type amino acid transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR030679; ABC_ATPase_HisP-typ.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..259
FT                   /note="L-cystine import ATP-binding protein TcyN"
FT                   /id="PRO_0000093145"
FT   DOMAIN          2..239
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   259 AA;  29562 MW;  8490055A2DE2706E CRC64;
     MIEIKNIHKQ FGIHHVLKGI NLTVRKGEVV TIIGPSGSGK TTFLRCLNLL ERPDEGIISI
     HDKVINCRFP SKKEVHWLRK QTAMVFQQYH LFAHKTVIEN VMEGLTIARK MRKQDAYAVA
     ENELRKVGLQ DKLNAYPSQL SGGQKQRVGI ARALAIHPDV LLFDEPTAAL DPELVGEVLE
     VMLEIVKTGA TMIVVTHEME FARRVSDQVV FMDEGVIVEQ GTPEEVFRHT KKDRTRQFLR
     RVSPEYLFEP KEHIKEPVI