FOCA_ECO57
ID FOCA_ECO57 Reviewed; 285 AA.
AC P0AC25; P21501;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable formate transporter 1;
DE AltName: Full=Formate channel 1;
GN Name=focA; OrderedLocusNames=Z1250, ECs0987;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Involved in the bidirectional transport of formate.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P0AC25; P0AC25: focA; NbExp=3; IntAct=EBI-15817706, EBI-15817706;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FNT transporter (TC 2.A.44) family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG55389.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34410.1; -; Genomic_DNA.
DR PIR; A85616; A85616.
DR PIR; C90752; C90752.
DR RefSeq; NP_309014.1; NC_002695.1.
DR RefSeq; WP_000642546.1; NZ_SWKA01000005.1.
DR PDB; 3KCU; X-ray; 2.24 A; A/B/C/D/E=1-285.
DR PDB; 3KCV; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J=1-285.
DR PDBsum; 3KCU; -.
DR PDBsum; 3KCV; -.
DR AlphaFoldDB; P0AC25; -.
DR SMR; P0AC25; -.
DR DIP; DIP-59304N; -.
DR STRING; 155864.EDL933_1167; -.
DR EnsemblBacteria; AAG55389; AAG55389; Z1250.
DR EnsemblBacteria; BAB34410; BAB34410; ECs_0987.
DR GeneID; 67414208; -.
DR GeneID; 917772; -.
DR KEGG; ece:Z1250; -.
DR KEGG; ecs:ECs_0987; -.
DR PATRIC; fig|386585.9.peg.1106; -.
DR eggNOG; COG2116; Bacteria.
DR HOGENOM; CLU_036896_3_0_6; -.
DR OMA; MIWFPIM; -.
DR EvolutionaryTrace; P0AC25; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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:0015499; F:formate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000292; For/NO2_transpt.
DR InterPro; IPR024002; For/NO2_transpt_CS.
DR InterPro; IPR023999; Formate_transptr_FocA_put.
DR PANTHER; PTHR30520; PTHR30520; 1.
DR Pfam; PF01226; Form_Nir_trans; 1.
DR TIGRFAMs; TIGR00790; fnt; 1.
DR TIGRFAMs; TIGR04060; formate_focA; 1.
DR PROSITE; PS01005; FORMATE_NITRITE_TP_1; 1.
DR PROSITE; PS01006; FORMATE_NITRITE_TP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..285
FT /note="Probable formate transporter 1"
FT /id="PRO_0000094718"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 31..56
FT /evidence="ECO:0007829|PDB:3KCU"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3KCU"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:3KCU"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3KCU"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 114..135
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3KCU"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 161..182
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:3KCU"
FT HELIX 255..278
FT /evidence="ECO:0007829|PDB:3KCU"
SQ SEQUENCE 285 AA; 30991 MW; E0B06FFFC362DE16 CRC64;
MKADNPFDLL LPAAMAKVAE EAGVYKATKH PLKTFYLAIT AGVFISIAFV FYITATTGTG
TMPFGMAKLV GGICFSLGLI LCVVCGADLF TSTVLIVVAK ASGRITWGQL AKNWLNVYFG
NLVGALLFVL LMWLSGEYMT ANGQWGLNVL QTADHKVHHT FIEAVCLGIL ANLMVCLAVW
MSYSGRSLMD KAFIMVLPVA MFVASGFEHS IANMFMIPMG IVIRDFASPE FWTAVGSAPE
NFSHLTVMNF ITDNLIPVTI GNIIGGGLLV GLTYWVIYLR ENDHH
