TCYM_BACSU
ID TCYM_BACSU Reviewed; 235 AA.
AC O34931;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=L-cystine transport system permease protein TcyM;
GN Name=tcyM; Synonyms=ytmM; OrderedLocusNames=BSU29350;
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, 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: Part of the ABC transporter complex TcyJKLMN involved in L-
CC cystine import. Probably responsible for the translocation of the
CC substrate across the membrane (Probable). Is also involved in
CC cystathionine, djenkolate, and S-methylcysteine transport.
CC {ECO:0000269|PubMed:15262924, ECO:0000305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for L-cystine {ECO:0000269|PubMed:15262924};
CC Vmax=0.5 nmol/min/mg enzyme for L-cystine transport
CC {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}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
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 binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; AF008220; AAC00328.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14895.1; -; Genomic_DNA.
DR PIR; G69996; G69996.
DR RefSeq; NP_390813.1; NC_000964.3.
DR RefSeq; WP_004398678.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34931; -.
DR SMR; O34931; -.
DR STRING; 224308.BSU29350; -.
DR TCDB; 3.A.1.3.13; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34931; -.
DR EnsemblBacteria; CAB14895; CAB14895; BSU_29350.
DR GeneID; 935938; -.
DR KEGG; bsu:BSU29350; -.
DR PATRIC; fig|224308.179.peg.3189; -.
DR eggNOG; COG0765; Bacteria.
DR InParanoid; O34931; -.
DR OMA; FWFNIGA; -.
DR PhylomeDB; O34931; -.
DR BioCyc; BSUB:BSU29350-MON; -.
DR SABIO-RK; O34931; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR043429; ArtM/GltK/GlnP/TcyL/YhdX-like.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR30614; PTHR30614; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..235
FT /note="L-cystine transport system permease protein TcyM"
FT /id="PRO_0000060275"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 15..220
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 235 AA; 25593 MW; 438AD7E40EC267BF CRC64;
MQFDFPFIVS AMKEMVKTIP LTLMMAVLPI VFGFLVALGN IIVRIFRIKG LVACSRFYVS
FFRSTPAILH IMLIYLGIPP VADQVSSFFH LGWSANEIPV SMFVIMALSL TAGAYLTEII
RSGILAMDTG QVEAAYSIGL TYSQTFRRVI LPQALKVSIP NFTNLGIGFL HTTSIAAIVA
VPEITGTATI VASDNYAFLE AFIGAAIIYW VLTLILESAN GVLERKAARF QGGTL
