SAM_RICTY
ID SAM_RICTY Reviewed; 294 AA.
AC Q68XV0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=S-adenosylmethionine uptake transporter;
GN Name=sam; OrderedLocusNames=RT0056;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
RN [2]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=12730161; DOI=10.1128/jb.185.10.3031-3035.2003;
RA Tucker A.M., Winkler H.H., Driskell L.O., Wood D.O.;
RT "S-adenosylmethionine transport in Rickettsia prowazekii.";
RL J. Bacteriol. 185:3031-3035(2003).
CC -!- FUNCTION: Transports S-adenosylmethionine.
CC {ECO:0000269|PubMed:12730161}.
CC -!- ACTIVITY REGULATION: Transport is inhibited by S-adenosylethionine and
CC to a lesser extent by S-adenosylhomocysteine. Unlike eukaryotic
CC transporters is not inhibited by sinfungin. Also inhibited by 2.4-
CC dinitrophenol, suggesting transport is an energy-dependent process.
CC {ECO:0000269|PubMed:12730161}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC superfamily. 10 TMS drug/metabolite exporter (DME) (TC 2.A.7.3) family.
CC {ECO:0000305}.
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DR EMBL; AE017197; AAU03542.1; -; Genomic_DNA.
DR RefSeq; WP_011190529.1; NC_006142.1.
DR AlphaFoldDB; Q68XV0; -.
DR SMR; Q68XV0; -.
DR STRING; 257363.RT0056; -.
DR EnsemblBacteria; AAU03542; AAU03542; RT0056.
DR KEGG; rty:RT0056; -.
DR eggNOG; COG0697; Bacteria.
DR HOGENOM; CLU_032828_0_0_5; -.
DR OMA; PFFWEVP; -.
DR OrthoDB; 1420919at2; -.
DR Proteomes; UP000000604; 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:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR000620; EamA_dom.
DR Pfam; PF00892; EamA; 2.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..294
FT /note="S-adenosylmethionine uptake transporter"
FT /id="PRO_0000280998"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 23..141
FT /note="EamA 1"
FT DOMAIN 160..280
FT /note="EamA 2"
SQ SEQUENCE 294 AA; 33141 MW; 34778945A87EF02A CRC64;
MNDALKTYLK GICWFLLSLV TSSVNDVISK YLGTRLHSFE VAFFRFLFSS IVLLPFVVYY
GKSTLKTRHP VIHVLRGLLL FFGMTSWTYG LTIAPVTTAT VISFSIPLFT LILAVFILNE
NIIWQRWVVT VVGFIGLVVM LKPHTKDFNP EILYLILAAI SFAMLDIINK KFVVKESMLS
MLFYSAIVTA IVSLPVSMEY WITPSSFELT LLFVLGSSGS FILFFLLKAF TMVDATATAP
YRYLELVISA IAAYFIFNEF PDKSTAHGAV IIIPATLFIM YSEKKSMSSK HESQ
