PANF_ECOLI
ID PANF_ECOLI Reviewed; 483 AA.
AC P16256; P76679; Q2M8V7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Sodium/pantothenate symporter {ECO:0000305};
DE AltName: Full=Pantothenate permease {ECO:0000303|PubMed:3888959};
GN Name=panF {ECO:0000303|PubMed:2193919}; OrderedLocusNames=b3258, JW3226;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2193919; DOI=10.1128/jb.172.7.3842-3848.1990;
RA Jackowski S., Alix J.-H.;
RT "Cloning, sequence, and expression of the pantothenate permease (panF) gene
RT of Escherichia coli.";
RL J. Bacteriol. 172:3842-3848(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RA Best E.A., Knauf V.C.;
RT "Cloning and characterization of the E. coli fabEG operon encoding subunits
RT of acetyl-CoA carboxylase.";
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 443-483.
RX PubMed=8226664; DOI=10.1128/jb.175.22.7178-7188.1993;
RA Vanet A., Plumbridge J.A., Alix J.-H.;
RT "Cotranscription of two genes necessary for ribosomal protein L11
RT methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-
RT 12.";
RL J. Bacteriol. 175:7178-7188(1993).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=3888959; DOI=10.1128/jb.162.3.1156-1161.1985;
RA Vallari D.S., Rock C.O.;
RT "Pantothenate transport in Escherichia coli.";
RL J. Bacteriol. 162:1156-1161(1985).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular
CC pantothenate. {ECO:0000269|PubMed:2193919, ECO:0000269|PubMed:3888959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantothenate(in) + Na(+)(in) = (R)-pantothenate(out) +
CC Na(+)(out); Xref=Rhea:RHEA:29927, ChEBI:CHEBI:29032,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:3888959};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29929;
CC Evidence={ECO:0000269|PubMed:3888959};
CC -!- ACTIVITY REGULATION: Pantothenate uptake is not reduced in osmotically
CC shocked cells or by ATP depletion with arsenate, but is reduced greater
CC than 90% by the dissipation of the membrane electrochemical gradient
CC with 2,4-dinitrophenol. {ECO:0000269|PubMed:3888959}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23747.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA58061.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M30953; AAA24276.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58061.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76290.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77299.1; -; Genomic_DNA.
DR EMBL; M83198; AAA23747.1; ALT_INIT; Genomic_DNA.
DR EMBL; S67010; AAB28768.1; -; Genomic_DNA.
DR RefSeq; NP_417724.4; NC_000913.3.
DR RefSeq; WP_001175728.1; NZ_SSZK01000034.1.
DR AlphaFoldDB; P16256; -.
DR SMR; P16256; -.
DR BioGRID; 4262451; 174.
DR DIP; DIP-10439N; -.
DR STRING; 511145.b3258; -.
DR TCDB; 2.A.21.1.1; the solute:sodium symporter (sss) family.
DR PaxDb; P16256; -.
DR PRIDE; P16256; -.
DR EnsemblBacteria; AAC76290; AAC76290; b3258.
DR EnsemblBacteria; BAE77299; BAE77299; BAE77299.
DR GeneID; 66672848; -.
DR GeneID; 947752; -.
DR KEGG; ecj:JW3226; -.
DR KEGG; eco:b3258; -.
DR PATRIC; fig|511145.12.peg.3357; -.
DR EchoBASE; EB0679; -.
DR eggNOG; COG4145; Bacteria.
DR HOGENOM; CLU_018808_15_1_6; -.
DR InParanoid; P16256; -.
DR OMA; GWWGMRR; -.
DR PhylomeDB; P16256; -.
DR BioCyc; EcoCyc:PANF-MON; -.
DR BioCyc; MetaCyc:PANF-MON; -.
DR PRO; PR:P16256; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015233; F:pantothenate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IDA:EcoCyc.
DR GO; GO:0015887; P:pantothenate transmembrane transport; IDA:EcoCyc.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IEA:InterPro.
DR CDD; cd10327; SLC5sbd_PanF; 1.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR011849; Na/pantothenate_symporter.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR018212; Na/solute_symporter_CS.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR02119; panF; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..483
FT /note="Sodium/pantothenate symporter"
FT /id="PRO_0000105402"
FT TOPO_DOM 1..2
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..73
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..157
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..232
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..305
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..391
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 179..206
FT /note="RASVLNDTMQGLVMLIGTVVLLIGVVHA -> APAAERHHARACDADWHRCA
FT AYWRSTC (in Ref. 1; AAA24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="P -> A (in Ref. 1; AAA24276)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="T -> H (in Ref. 1; AAA24276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 51717 MW; 5F607C043ECAB1F8 CRC64;
MQLEVILPLV AYLVVVFGIS VYAMRKRSTG TFLNEYFLGS RSMGGIVLAM TLTATYISAS
SFIGGPGAAY KYGLGWVLLA MIQLPAVWLS LGILGKKFAI LARRYNAVTL NDMLFARYQS
RLLVWLASLS LLVAFVGAMT VQFIGGARLL ETAAGIPYET GLLIFGISIA LYTAFGGFRA
SVLNDTMQGL VMLIGTVVLL IGVVHAAGGL SNAVQTLQTI DPQLVTPQGA DDILSPAFMT
SFWVLVCFGV IGLPHTAVRC ISYKDSKAVH RGIIIGTIVV AILMFGMHLA GALGRAVIPD
LTVPDLVIPT LMVKVLPPFA AGIFLAAPMA AIMSTINAQL LQSSATIIKD LYLNIRPDQM
QNETRLKRMS AVITLVLGAL LLLAAWKPPE MIIWLNLLAF GGLEAVFLWP LVLGLYWERA
NAKGALSAMI VGGVLYAVLA TLNIQYLGFH PIVPSLLLSL LAFLVGNRFG TSVPQATVLT
TDK
