ID C0M9I7_STRE4 Unreviewed; 304 AA.
AC C0M9I7;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Di-tripeptide transport system permease protein {ECO:0000313|EMBL:CAW92476.1};
DE Flags: Precursor;
GN OrderedLocusNames=SEQ_0353 {ECO:0000313|EMBL:CAW92476.1};
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482 {ECO:0000313|EMBL:CAW92476.1, ECO:0000313|Proteomes:UP000001365};
RN [1] {ECO:0000313|EMBL:CAW92476.1, ECO:0000313|Proteomes:UP000001365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047 {ECO:0000313|EMBL:CAW92476.1,
RC ECO:0000313|Proteomes:UP000001365};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000256|RuleBase:RU363032}.
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DR EMBL; FM204883; CAW92476.1; -; Genomic_DNA.
DR RefSeq; WP_012678996.1; NC_012471.1.
DR AlphaFoldDB; C0M9I7; -.
DR KEGG; seu:SEQ_0353; -.
DR HOGENOM; CLU_036879_1_2_9; -.
DR OrthoDB; 9773683at2; -.
DR Proteomes; UP000001365; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR43163; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR PANTHER; PTHR43163:SF6; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 227..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 271..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 93..294
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 304 AA; 33374 MW; 0C28A7BE006CEE1C CRC64;
MIKYLLKRVA ILVVTLWVVI TLSFFLMQVM PGTPYNSPKL TDDMIAMLNQ QYGLDKPLWQ
QYLKYLFDIL HGDFGTSYQS INQSVTTLIS QRLGVSVHLG VQALIVGISS GLAVGAVSAR
NKNNSIDAIL SVISTLGISM PSFIIGLLLL DYLGFKWNLL PLSGWGSFGQ TILPTLALAI
PVFAQVTRFF RSEMIETLST DYIQLARAKG LTKRQVTRRH AYRNSMIPVL TLVGPMAAGI
LTGSALIEQI FSIPGIGQQF VTSIPTKDYP VIMGTTIVYA LMLMVAILAT DMIISIADPR
VRLG
//
