BRNQL_STAAR
ID BRNQL_STAAR Reviewed; 447 AA.
AC Q6GH01;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Putative branched-chain amino acid carrier protein SAR1419;
GN OrderedLocusNames=SAR1419;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Component of the transport system for branched-chain amino
CC acids (leucine, isoleucine and valine), which is coupled to a proton
CC motive force (Potential). Contributes to NaCl tolerance (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the branched chain amino acid transporter
CC family. {ECO:0000305}.
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DR EMBL; BX571856; CAG40416.1; -; Genomic_DNA.
DR RefSeq; WP_001039267.1; NC_002952.2.
DR AlphaFoldDB; Q6GH01; -.
DR KEGG; sar:SAR1419; -.
DR HOGENOM; CLU_036807_0_1_9; -.
DR OMA; IWPAGPI; -.
DR OrthoDB; 1533843at2; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015658; F:branched-chain amino acid transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR004685; Brnchd-chn_aa_trnsp_Livcs.
DR PANTHER; PTHR30588; PTHR30588; 1.
DR Pfam; PF05525; Branch_AA_trans; 1.
DR TIGRFAMs; TIGR00796; livcs; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..447
FT /note="Putative branched-chain amino acid carrier protein
FT SAR1419"
FT /id="PRO_0000294013"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 447 AA; 48893 MW; 4CDC138B4A8400D9 CRC64;
MNKNTWVIGF TLFAMFFGAG NLIFPPNLGL DSGQFFWPAI LAFVLTGIGL PLLGVIVGAL
DKEGYIGALN KISPKFSILF LIIIYLTIGP LFAIPRTAST SFEMTITPII HSNSSIALFI
FTIIYFIVVL YICLNPSKLI DRIGSLLTPL LLITILAMII KAYLDFSGNS AGKGNEALYH
SNFSSFAEGF TQGYLTMDAI AAIAFSMIVV NAVKLTGITK TNQIFKQTLT AGLIAAIALI
FIYISLGYIG NHMPVSDMKL NELKSHDRNI GTYLLTTMAS TGFGSFGKYL LGIIVALACL
TTACGLIVAV SEYFHRIVPK VSYKAFVLVF ILMSFIIANQ GLNAVISMSI PVLSIVYPVA
ITVVLLILIA KFIPTKRITQ QIPVIIVFIL SIFSVISKLG WLKINFIESL PLRAYSLEWF
PVAIIATILG YLVGIFVKQD PIKYQQE