DTPB_ALIFM
ID DTPB_ALIFM Reviewed; 495 AA.
AC B5FDK5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Dipeptide and tripeptide permease B {ECO:0000255|HAMAP-Rule:MF_01879};
GN Name=dtpB {ECO:0000255|HAMAP-Rule:MF_01879}; OrderedLocusNames=VFMJ11_1199;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001139; ACH65837.1; -; Genomic_DNA.
DR RefSeq; WP_012533315.1; NC_011184.1.
DR AlphaFoldDB; B5FDK5; -.
DR SMR; B5FDK5; -.
DR EnsemblBacteria; ACH65837; ACH65837; VFMJ11_1199.
DR KEGG; vfm:VFMJ11_1199; -.
DR HOGENOM; CLU_004790_0_0_6; -.
DR OMA; IFFIELW; -.
DR Proteomes; UP000001857; Chromosome I.
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; PS01023; PTR2_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..495
FT /note="Dipeptide and tripeptide permease B"
FT /id="PRO_0000395189"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 38..50
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 72..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 102..104
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 126..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 166..170
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 192..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 231
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 253..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 287..309
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 331..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 370..373
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 395..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 431..454
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
FT TOPO_DOM 476..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01879"
SQ SEQUENCE 495 AA; 54151 MW; 15C949B9553904FB CRC64;
MDNKVSILNQ PKPFKMIFFI ELWERFGYYG LQGILAVYFV DKLGFSMQDS FVTFGAFAAL
VYGLVSVGGY VGDYVLGTKR TMVFGAVVLA LGYFLMGFSI LNPNFIYVAL GAIAVGNGLF
KANPSSLLAK CYEKGDSRLD GAFTLYYMSI NIGSLVSLSI SPVIANNYGY EYAFIICGLG
LIASLFSYFS LRSTVQGIGS EPDALPLNKT KALIVLIGTI ASTLVCAWLL QNIMMANLAL
GLIGVGVVGF FLKETFKEVG EQRNKMIVAF ILMLQAIIFY VLYAQMPTSL NFFAINNVHS
ELFGMDINPV SLQALNPFWV IFCSPILAYL YTYYGNQNKD LSMPGKFTVG MFMCAFGFLS
VAAAGNWFAD QAGMVSVWWM VLVYLFQSLG ELMISGLGLA MVASLVPQRL MGFTMGAWFL
TQAASFIIGG YVATFSATPE HLTDPLDTLP VYTELFQNIG FVTLAVAIVM AITAPKLNKM
MTSSQPEDAE LVEQP
