PEPT_YERP4
ID PEPT_YERP4 Reviewed; 511 AA.
AC A0A2R9TD79; A0A0M3KKZ1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Peptide transporter YePEPT {ECO:0000303|PubMed:26246134};
GN ORFNames=YEP4_02370 {ECO:0000312|EMBL:EOR83458.1};
OS Yersinia enterocolitica subsp. palearctica serotype O:3 (strain YE-P4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=1329364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE-P4;
RX PubMed=23846271; DOI=10.1128/genomea.00466-13;
RA Garzetti D., Heesemann J., Rakin A.;
RT "Genome sequences of four Yersinia enterocolitica bioserotype 4/O:3
RT isolates from mammals.";
RL Genome Announc. 1:E00466-E00466(2013).
RN [2] {ECO:0007744|PDB:4W6V}
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS), FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP MUTAGENESIS OF PHE-311 AND LYS-314.
RC STRAIN=YE-P4;
RX PubMed=26246134; DOI=10.1186/s12915-015-0167-8;
RA Boggavarapu R., Jeckelmann J.M., Harder D., Ucurum Z., Fotiadis D.;
RT "Role of electrostatic interactions for ligand recognition and specificity
RT of peptide transporters.";
RL BMC Biol. 13:58-58(2015).
CC -!- FUNCTION: Mediates the proton-dependent uptake of dipeptides. Shows
CC higher affinity for dipeptides with a negatively charged amino acid
CC residue at the N-terminal position, such as Asp-Ala and Glu-Ala. Also
CC displays specificity for Ala-Ala, Ala-Tyr and Tyr-Ala.
CC {ECO:0000269|PubMed:26246134}.
CC -!- ACTIVITY REGULATION: Transport is inhibited by the proton ionophore
CC carbonyl cyanide m-chlorophenylhydrazone (CCCP).
CC {ECO:0000269|PubMed:26246134}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=199 uM for Ala-Ala {ECO:0000269|PubMed:26246134};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:26246134}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:26246134}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; ASHU01000009; EOR83458.1; -; Genomic_DNA.
DR RefSeq; WP_005157856.1; NZ_ASHU01000009.1.
DR PDB; 4W6V; X-ray; 3.02 A; A=1-511.
DR PDB; 7Q0L; X-ray; 2.71 A; A=1-511.
DR PDB; 7Q0M; X-ray; 2.54 A; A=1-511.
DR PDBsum; 4W6V; -.
DR PDBsum; 7Q0L; -.
DR PDBsum; 7Q0M; -.
DR AlphaFoldDB; A0A2R9TD79; -.
DR SMR; A0A2R9TD79; -.
DR EnsemblBacteria; EOR83458; EOR83458; YEP4_02370.
DR Proteomes; UP000014202; Unassembled WGS sequence.
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:1904680; F:peptide transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006857; P:oligopeptide transport; IEA:InterPro.
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 InterPro; IPR005279; Dipep/tripep_permease.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00924; yjdL_sub1_fam; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Peptide transport; Protein transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..511
FT /note="Peptide transporter YePEPT"
FT /id="PRO_0000450336"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 46..59
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 60..84
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 85..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 110..115
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 139..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 150..175
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 176..181
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 182..208
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 209..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 254..256
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 280..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..321
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 322..335
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 336..357
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 358..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..396
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 397..405
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 427..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 463..471
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 472..496
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:26246134"
FT TOPO_DOM 497..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26246134"
FT MUTAGEN 311
FT /note="F->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:26246134"
FT MUTAGEN 314
FT /note="K->A: Abolishes specificity for charged residues."
FT /evidence="ECO:0000269|PubMed:26246134"
FT MUTAGEN 314
FT /note="K->E: Loses the specificity for negatively charged
FT amino acids in the N-terminal position and acquires
FT specificity for dipeptides with a positively charged amino
FT acid side chain in that position."
FT /evidence="ECO:0000269|PubMed:26246134"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:4W6V"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:4W6V"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:4W6V"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 88..108
FT /evidence="ECO:0007829|PDB:4W6V"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 115..142
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 150..179
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 182..202
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:4W6V"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 233..252
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 258..282
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 288..311
FT /evidence="ECO:0007829|PDB:4W6V"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:4W6V"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 371..399
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 407..423
FT /evidence="ECO:0007829|PDB:4W6V"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:4W6V"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 443..461
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:4W6V"
FT HELIX 473..499
FT /evidence="ECO:0007829|PDB:4W6V"
SQ SEQUENCE 511 AA; 55499 MW; 116A0EAA37BD72BF CRC64;
MQTSTNTPGG RTFFGHPYPL SGLFLSEMWE RFSFYGIRPL LILFMAATVF DGGMGLPREQ
ASAIVGIFAG SMYLAALPGG LLADNWLGQQ RAVWYGSILI ALGHLSIALS AFFGNDLFFI
GLVFIVLGTG LFKTCISVMV GTLYKPGDAR RDGGFSLFYM GINMGSFIAP LLSGWLLRTH
GWHWGFGIGG IGMLVALLIF RGFAIPAMKR YDAEVGLDSS WNKPTNQRQG VGRWVTAIMA
VVVVIIALIS QGVIPINPVM IASLLVYVIA ASVTLYFIYL FAFAKMSRKD RARLLVCFIL
LVSAAFFWSA FEQKPTSFNL FANDYTDRMV MGFEIPTVWF QSINALFIIL LAPVFSWAWP
ALAKKKIQPS SITKFVIGIL CAAAGFAVMM YAAQHVLSSG GAGVSPLWLV MSILLLTLGE
LCLSPIGLAT MTLLAPDRMR GQVMGLWFCA SSLGNLAAGL IGGHVKADQL DMLPTLFARC
SIALVICAAV LILLIVPIRR LMNNTQGQQT A
