DTPA_CHRVO
ID DTPA_CHRVO Reviewed; 495 AA.
AC Q7NRM5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Dipeptide and tripeptide permease A {ECO:0000255|HAMAP-Rule:MF_01878};
GN Name=dtpA {ECO:0000255|HAMAP-Rule:MF_01878}; OrderedLocusNames=CV_3755;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
CC -!- FUNCTION: Proton-dependent permease that transports di- and
CC tripeptides. {ECO:0000255|HAMAP-Rule:MF_01878}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01878}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01878}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01878}.
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DR EMBL; AE016825; AAQ61417.1; -; Genomic_DNA.
DR RefSeq; WP_011137302.1; NC_005085.1.
DR AlphaFoldDB; Q7NRM5; -.
DR SMR; Q7NRM5; -.
DR STRING; 243365.CV_3755; -.
DR EnsemblBacteria; AAQ61417; AAQ61417; CV_3755.
DR KEGG; cvi:CV_3755; -.
DR eggNOG; COG3104; Bacteria.
DR HOGENOM; CLU_004790_0_0_4; -.
DR OMA; QYATFFT; -.
DR OrthoDB; 470322at2; -.
DR Proteomes; UP000001424; 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_01878; PTR2_DtpA_subfam; 1.
DR InterPro; IPR023517; AA/pep_transptr_DtpA.
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 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..495
FT /note="Dipeptide and tripeptide permease A"
FT /id="PRO_0000395172"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 42..51
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 73..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 124..145
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 167..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 193..209
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 231..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 254..266
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 288..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 334..344
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 366..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 397..409
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 431..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
FT TOPO_DOM 473..495
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01878"
SQ SEQUENCE 495 AA; 53668 MW; CD434C886F6540E2 CRC64;
MTTSALNPLR QPKPFYLIFS IEFWERFGFY GLQGILAVYL VKALGLREAD SFTLFSSFIA
LVYGLIAVGG WLGDKVLGTK RTILLGALVL TAGYAMVTAS SEHISLLYLG MGTIAVGNGL
FKANPSSLLS KCYEENDPRL DGAFTMYYMA INIGSLLSML ATPWLADQFG YAHAFALSVV
GMLITVANFI LMQGWVKNYG SDADFRTPRL STWLAVLAGV VAACAAAALL LKHEIIANVV
LAVLSIGVVG LYVKETLLLK GAERKKMIVA AILMLQATVF FVLYNQMPLS LNFFAIHNTE
HMLFGIPVQP EQFQSLNPFW IMLASPLLAL CYNKLGNRLP MPHKFAIGMV LCAGAFLVLP
LGAKYANAQG LVSSNWMVLS YLLQSVGELL ISGLGLAMVA QLVPQRLMGF IMGAWFLTSA
ASSVIAGWVA GLTAAPDNVT NPLATLEIYS RVFTQIGVVT GVIAVVTIII APWLHRMTLD
EKPAHPEHEM ALDAR
