DTPB_SHIDS
ID DTPB_SHIDS Reviewed; 489 AA.
AC Q32AW5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Dipeptide and tripeptide permease B {ECO:0000255|HAMAP-Rule:MF_01879};
GN Name=dtpB {ECO:0000255|HAMAP-Rule:MF_01879}; OrderedLocusNames=SDY_3566;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Proton-dependent permease that transports di- and
CC tripeptides. {ECO:0000255|HAMAP-Rule:MF_01879}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01879}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01879}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01879}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB63540.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP000034; ABB63540.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q32AW5; -.
DR SMR; Q32AW5; -.
DR STRING; 300267.SDY_3566; -.
DR EnsemblBacteria; ABB63540; ABB63540; SDY_3566.
DR KEGG; sdy:SDY_3566; -.
DR HOGENOM; CLU_004790_0_0_6; -.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015333; F:peptide:proton symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd17346; MFS_DtpA_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR HAMAP; MF_01879; PTR2_DtpB_subfam; 1.
DR InterPro; IPR023778; AA/pep_transptr_DtpB.
DR InterPro; IPR005279; Dipep/tripep_permease.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR PANTHER; PTHR11654:SF102; PTHR11654:SF102; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00924; yjdL_sub1_fam; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..489
FT /note="Dipeptide and tripeptide permease B"
FT /id="PRO_0000395188"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 49..52
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 74..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 104..106
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 128..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 168..172
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 194..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 232..233
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 255..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 289..311
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 333..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 372..380
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 402..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 433..456
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 478..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
SQ SEQUENCE 489 AA; 53325 MW; 549875B688CC5FC7 CRC64;
MNTTTPMGML QQPRPFFMIF FVELWERFGY YGVQGVLAVF FVKQLGFSQE QAFVTFGAFA
ALVYGLISIG GYVGDHLLGT KRTIVLGALV LAIGYFMTGL SLLKPDLIFI ALGTIAVGNG
LFKANPASLL SKCYPPKAPR LDGAFTLFYM SINIGSLIAL SLAPVIADRF GYSVTYNLCG
AGLIIALLVY IACRGMVKDI GSEPDFRPMS FSKLLYVLLG SVVMIFVCAW LMHNVEVANL
VLIVLSIVVT IIFFRQAFKL DKTGRNKMFV AFVLMLEAVV FYILYAQMPT SLNFFAINNV
HHEILGFSIN PVSFQALNPF WVVLASPILA GIYTHLGSKG KDLSMPMKFT LGMFMCSLGF
LTAAAAGMWF ADAQGLTSPW FIVLVYLFQS LGELFISALG LAMVAALVPQ HLMGFILGIS
FLTQAAAFLL GGYVATFTAV PDNITDPLET LPVYTNVFGK IGLVTLGVAV VMLLMVPWLK
RMIAAPESH
