POTE_HAEIN
ID POTE_HAEIN Reviewed; 435 AA.
AC P44768;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Putrescine transporter PotE {ECO:0000255|HAMAP-Rule:MF_02073};
DE AltName: Full=Putrescine-proton symporter / putrescine-ornithine antiporter {ECO:0000255|HAMAP-Rule:MF_02073};
GN Name=potE {ECO:0000255|HAMAP-Rule:MF_02073}; OrderedLocusNames=HI_0590;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes both the uptake and excretion of putrescine. The
CC uptake of putrescine is dependent on the membrane potential and the
CC excretion involves putrescine-ornithine antiporter activity.
CC {ECO:0000255|HAMAP-Rule:MF_02073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + putrescine(in) = H(+)(out) + putrescine(out);
CC Xref=Rhea:RHEA:28891, ChEBI:CHEBI:15378, ChEBI:CHEBI:326268;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine(out) + putrescine(in) = L-ornithine(in) +
CC putrescine(out); Xref=Rhea:RHEA:28827, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:326268; Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02073}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02073}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2)
CC family. {ECO:0000255|HAMAP-Rule:MF_02073}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC22247.1; -; Genomic_DNA.
DR PIR; E64079; E64079.
DR RefSeq; NP_438748.1; NC_000907.1.
DR RefSeq; WP_005694562.1; NC_000907.1.
DR AlphaFoldDB; P44768; -.
DR SMR; P44768; -.
DR STRING; 71421.HI_0590; -.
DR EnsemblBacteria; AAC22247; AAC22247; HI_0590.
DR KEGG; hin:HI_0590; -.
DR PATRIC; fig|71421.8.peg.612; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_0_6; -.
DR OMA; AEKVMSV; -.
DR PhylomeDB; P44768; -.
DR BioCyc; HINF71421:G1GJ1-602-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015496; F:putrescine:ornithine antiporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR HAMAP; MF_02073; Putrescine_transp; 1.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004754; Amino_acid_antiprt.
DR InterPro; IPR027566; Symport/antiport_PotE.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00905; 2A0302; 1.
DR TIGRFAMs; TIGR04299; antiport_PotE; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..435
FT /note="Putrescine transporter PotE"
FT /id="PRO_0000054252"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
SQ SEQUENCE 435 AA; 46349 MW; C4D992217975B5A8 CRC64;
MSAKSNKIGV VQLTILTMVN MMGSGIIMLP TKLAEIGTIS IVSWLVTAVG STALAYAFAQ
CGMFSKKSGG MGGYAEYSFG KAGNFMANYT YGVSLVIANT AIAISAVGYG SELFGTILSP
LSIALWTIFT LWLATVLNFG GARITGNISS FTIWGVIIPV VGISIIGWKW FDGSMYVNSW
NPHNVPTFEA IGVSISMTLW AFLGLESACA NADAVENPEK NVPIAVLGGT LGAAVIYIVS
TNVIAGIVPN LELANSTAPF GLAFAHMFDE TVGKVIMGLM VMSCFGSLLG WQFTIAQVFK
SSAEEGYFPA FFKKITSKDA PVVGMITITA LQTLLSLMTI SPSLNKQFNV LVDLAVVTNV
IPYLLSMAAL AVLLKAENVA PQKYKTTVFV AFIGSLYSIY ALYAAGEQAM LYGSIVTFIG
WTLYGFVSYK FDLKK