THRE_MYCTU
ID THRE_MYCTU Reviewed; 529 AA.
AC O69704; I6YH16; L0TDN2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable threonine/serine exporter {ECO:0000250|UniProtKB:H7C6B6};
GN OrderedLocusNames=Rv3737 {ECO:0000312|EMBL:CCP46564.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION IN VIRULENCE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=35287590; DOI=10.1186/s12879-021-06967-y;
RA Li Q., Peng Z., Fu X., Wang H., Zhao Z., Pang Y., Chen L.;
RT "Rv3737 is required for Mycobacterium tuberculosis growth in vitro and in
RT vivo and correlates with bacterial load and disease severity in human
RT tuberculosis.";
RL BMC Infect. Dis. 22:256-256(2022).
CC -!- FUNCTION: Catalyzes the export of L-threonine and L-serine from the
CC cell to the extracellular environment (By similarity). Export is
CC dependent on the proton motive force (By similarity). Required for in
CC vitro growth and survival of bacteria inside macrophages
CC (PubMed:35287590). {ECO:0000250|UniProtKB:H7C6B6,
CC ECO:0000269|PubMed:35287590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-threonine(in) = H(+)(in) + L-threonine(out);
CC Xref=Rhea:RHEA:28995, ChEBI:CHEBI:15378, ChEBI:CHEBI:57926;
CC Evidence={ECO:0000250|UniProtKB:H7C6B6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28996;
CC Evidence={ECO:0000250|UniProtKB:H7C6B6};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is significantly increased in clinical isolates
CC (PubMed:35287590). Expression level is positively correlated with lung
CC cavity number of TB patients (PubMed:35287590).
CC {ECO:0000269|PubMed:35287590}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant exhibits decreased growth rate
CC compared to wild-type strain in standard culture medium
CC (PubMed:35287590). In addition, the mutant shows decreased survival
CC rate in macrophages (PubMed:35287590). Infected macrophages produce a
CC significantly higher level of TNF-alpha and IL-6 mRNA expression
CC (PubMed:35287590). {ECO:0000269|PubMed:35287590}.
CC -!- SIMILARITY: Belongs to the ThrE exporter (TC 2.A.79) family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46564.1; -; Genomic_DNA.
DR RefSeq; NP_218254.1; NC_000962.3.
DR RefSeq; WP_003912272.1; NZ_NVQJ01000009.1.
DR AlphaFoldDB; O69704; -.
DR STRING; 83332.Rv3737; -.
DR PaxDb; O69704; -.
DR PRIDE; O69704; -.
DR DNASU; 885794; -.
DR GeneID; 885794; -.
DR KEGG; mtu:Rv3737; -.
DR PATRIC; fig|83332.111.peg.4157; -.
DR TubercuList; Rv3737; -.
DR eggNOG; COG2966; Bacteria.
DR eggNOG; COG3610; Bacteria.
DR OMA; MLSCGTG; -.
DR PhylomeDB; O69704; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR010619; ThrE.
DR InterPro; IPR024528; ThrE_2.
DR Pfam; PF06738; ThrE; 1.
DR Pfam; PF12821; ThrE_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..529
FT /note="Probable threonine/serine exporter"
FT /id="PRO_0000456292"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 529 AA; 54775 MW; 20B982BC267F20D6 CRC64;
MDQDRSDNTA LRRGLRIALR GRRDPLPVAG RRSRTSGGID DLHTRKVLDL TIRLAEVMLS
SGSGTADVVA TAQDVAQAYQ LTDCVVDITV TTIIVSALAT TDTPPVTIMR SVRTRSTDYS
RLAELDRLVQ RITSGGVAVD QAHEAMDELT ERPHPYPRWL ATAGAAGFAL GVAMLLGGTW
LTCVLAAVTS GVIDRLGRLL NRIGTPLFFQ RVFGAGIATL VAVAAYLIAG QDPTALVATG
IVVLLSGMTL VGSMQDAVTG YMLTALARLG DALFLTAGIV VGILISLRGV TNAGIQIELH
VDATTTLATP GMPLPILVAV SGAALSGVCL TIASYAPLRS VATAGLSAGL AELVLIGLGA
AGFGRVVATW TAAIGVGFLA TLISIRRQAP ALVTATAGIM PMLPGLAVFR AVFAFAVNDT
PDGGLTQLLE AAATALALGS GVVLGEFLAS PLRYGAGRIG DLFRIEGPPG LRRAVGRVVR
LQPAKSQQPT GTGGQRWRSV ALEPTTADDV DAGYRGDWPA TCTSATEVR
