OXLT_OXAFO
ID OXLT_OXAFO Reviewed; 418 AA.
AC Q51330;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Oxalate:formate antiporter;
DE Short=OFA;
DE AltName: Full=Oxalate:formate antiport protein;
DE AltName: Full=Oxalate:formate exchange protein;
GN Name=oxlT;
OS Oxalobacter formigenes.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=OxB;
RX PubMed=8636101; DOI=10.1074/jbc.271.12.6789;
RA Abe K., Ruan Z.-S., Maloney P.C.;
RT "Cloning, sequencing and expression in Escherichia coli of OxlT, the
RT oxalate:formate exchange protein of Oxalobacter formigenes.";
RL J. Biol. Chem. 271:6789-6793(1996).
RN [2]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF CYS-28; CYS-271;
RP GLY-349; LYS-355; GLY-362 AND GLY-363.
RC STRAIN=OxB;
RX PubMed=9651403; DOI=10.1074/jbc.273.28.17962;
RA Fu D., Maloney P.C.;
RT "Structure-function relationships in OxlT, the oxalate/formate transporter
RT of Oxalobacter formigenes. Topological features of transmembrane helix 11
RT as visualized by site-directed fluorescent labeling.";
RL J. Biol. Chem. 273:17962-17967(1998).
RN [3]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF GLN-56; PHE-59; GLN-66
RP AND SER-69.
RC STRAIN=OxB;
RX PubMed=11919184; DOI=10.1074/jbc.m111140200;
RA Ye L., Maloney P.C.;
RT "Structure/function relationships in OxlT, the oxalate/formate antiporter
RT of Oxalobacter formigenes. Assignment of transmembrane helix 2 to the
RT translocation pathway.";
RL J. Biol. Chem. 277:20372-20378(2002).
RN [4]
RP STRUCTURAL CHARACTERIZATION, AND MUTAGENESIS OF LYS-355.
RC STRAIN=OxB;
RX PubMed=11113128; DOI=10.1074/jbc.m008417200;
RA Fu D., Sarker R.I., Abe K., Bolton E., Maloney P.C.;
RT "Structure/function relationships in OxlT, the oxalate-formate transporter
RT of Oxalobacter formigenes. Assignment of transmembrane helix 11 to the
RT translocation pathway.";
RL J. Biol. Chem. 276:8753-8760(2001).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=OxB;
RX PubMed=11274108; DOI=10.1128/jb.183.8.2490-2496.2001;
RA Ye L., Jia Z., Jung T., Maloney P.C.;
RT "Topology of OxlT, the oxalate transporter of Oxalobacter formigenes,
RT determined by site-directed fluorescence labeling.";
RL J. Bacteriol. 183:2490-2496(2001).
RN [6]
RP CRYSTALLIZATION, AND DOMAIN.
RC STRAIN=OxB;
RX PubMed=11500368; DOI=10.1093/emboj/20.16.4408;
RA Heymann J.A.W., Sarker R., Hirai T., Shi D., Milne J.L.S., Maloney P.C.,
RA Subramaniam S.;
RT "Projection structure and molecular architecture of OxlT, a bacterial
RT membrane transporter.";
RL EMBO J. 20:4408-4413(2001).
CC -!- FUNCTION: Anion transporter that carries out the exchange of divalent
CC oxalate with monovalent formate, the product of oxalate
CC decarboxylation, at the plasma membrane, and in doing so catalyzes the
CC vectorial portion of a proton-motive metabolic cycle that drives ATP
CC synthesis. {ECO:0000269|PubMed:8636101}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11274108,
CC ECO:0000269|PubMed:11919184, ECO:0000269|PubMed:8636101,
CC ECO:0000269|PubMed:9651403}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11274108, ECO:0000269|PubMed:11919184,
CC ECO:0000269|PubMed:8636101, ECO:0000269|PubMed:9651403}.
CC -!- DOMAIN: The protein has a two-fold symmetry axis, with a central cavity
CC which may be associated with substrate transport. Residues contributed
CC from seven transmembrane helices probably line the substrate transport
CC pathway. {ECO:0000269|PubMed:11500368}.
CC -!- MISCELLANEOUS: Its velocity of transport is the highest one known so
CC far among transporters of organic molecules.
CC {ECO:0000305|PubMed:8636101}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. OFA (TC
CC 2.A.1.11) family. {ECO:0000305}.
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DR EMBL; U40075; AAC43722.1; -; Genomic_DNA.
DR PIR; T47239; T47239.
DR RefSeq; WP_005881678.1; NZ_CP042242.1.
DR AlphaFoldDB; Q51330; -.
DR SMR; Q51330; -.
DR TCDB; 2.A.1.11.1; the major facilitator superfamily (mfs).
DR KEGG; ofo:BRW83_0588; -.
DR BioCyc; MetaCyc:MON-16176; -.
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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR026355; Oxa/Form_antiport.
DR InterPro; IPR004741; Oxa_For_antiport_fam_transptr.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00890; 2A0111; 1.
DR TIGRFAMs; TIGR04259; oxa_formateAnti; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Ion transport; Membrane; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8636101"
FT CHAIN 2..418
FT /note="Oxalate:formate antiporter"
FT /id="PRO_0000173450"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 355
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000255"
FT MUTAGEN 28
FT /note="C->G: Slight decrease in activity; when associated
FT with A-271."
FT /evidence="ECO:0000269|PubMed:9651403"
FT MUTAGEN 56
FT /note="Q->C: Residual activity."
FT /evidence="ECO:0000269|PubMed:11919184"
FT MUTAGEN 59
FT /note="F->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11919184"
FT MUTAGEN 66
FT /note="Q->C: Residual activity."
FT /evidence="ECO:0000269|PubMed:11919184"
FT MUTAGEN 69
FT /note="S->C: Residual activity."
FT /evidence="ECO:0000269|PubMed:11919184"
FT MUTAGEN 271
FT /note="C->A: Slight decrease in activity; when associated
FT with G-28."
FT /evidence="ECO:0000269|PubMed:9651403"
FT MUTAGEN 349
FT /note="G->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9651403"
FT MUTAGEN 354
FT /note="A->C: Residual activity."
FT MUTAGEN 355
FT /note="K->C,G,Q,T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11113128,
FT ECO:0000269|PubMed:9651403"
FT MUTAGEN 355
FT /note="K->R: Residual activity."
FT /evidence="ECO:0000269|PubMed:11113128,
FT ECO:0000269|PubMed:9651403"
FT MUTAGEN 362
FT /note="G->C: Residual activity."
FT /evidence="ECO:0000269|PubMed:9651403"
FT MUTAGEN 363
FT /note="G->C: Residual activity."
FT /evidence="ECO:0000269|PubMed:9651403"
SQ SEQUENCE 418 AA; 44517 MW; CFF66C92EE23CB72 CRC64;
MNNPQTGQST GLLGNRWFYL VLAVLLMCMI SGVQYSWTLY ANPVKDNLGV SLAAVQTAFT
LSQVIQAGSQ PGGGYFVDKF GPRIPLMFGG AMVLAGWTFM GMVDSVPALY ALYTLAGAGV
GIVYGIAMNT ANRWFPDKRG LASGFTAAGY GLGVLPFLPL ISSVLKVEGV GAAFMYTGLI
MGILIILIAF VIRFPGQQGA KKQIVVTDKD FNSGEMLRTP QFWVLWTAFF SVNFGGLLLV
ANSVPYGRSL GLAAGVLTIG VSIQNLFNGG CRPFWGFVSD KIGRYKTMSV VFGINAVVLA
LFPTIAALGD VAFIAMLAIA FFTWGGSYAL FPSTNSDIFG TAYSARNYGF FWAAKATASI
FGGGLGAAIA TNFGWNTAFL ITAITSFIAF ALATFVIPRM GRPVKKMVKL SPEEKAVH
