BICA_SYNP2
ID BICA_SYNP2 Reviewed; 566 AA.
AC Q14SY0;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Bicarbonate transporter BicA;
GN Name=bicA; OrderedLocusNames=SYNPCC7002_A2371;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Nomura C.T., Persson S., Zhao J., Bryant D.A.;
RT "An analysis of forty genes encoding electron transport proteins from
RT Synechococcus sp. PCC 7002: a comparative study of electron transport
RT proteins from cyanobacteria and chloroplasts.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=15596724; DOI=10.1073/pnas.0405211101;
RA Price G.D., Woodger F.J., Badger M.R., Howitt S.M., Tucker L.;
RT "Identification of a SulP-type bicarbonate transporter in marine
RT cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18228-18233(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX PubMed=19951076; DOI=10.3109/09687680903400120;
RA Shelden M.C., Howitt S.M., Price G.D.;
RT "Membrane topology of the cyanobacterial bicarbonate transporter, BicA, a
RT member of the SulP (SLC26A) family.";
RL Mol. Membr. Biol. 27:12-23(2010).
CC -!- FUNCTION: Low/medium affinity, Na(+)-dependent bicarbonate transporter.
CC {ECO:0000269|PubMed:15596724}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:19951076}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19951076}.
CC -!- INDUCTION: Induced by CO(2). {ECO:0000269|PubMed:15596724}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; AF381039; ABG46427.1; -; Genomic_DNA.
DR EMBL; CP000951; ACB00349.1; -; Genomic_DNA.
DR RefSeq; WP_012307967.1; NC_010475.1.
DR AlphaFoldDB; Q14SY0; -.
DR SMR; Q14SY0; -.
DR STRING; 32049.SYNPCC7002_A2371; -.
DR TCDB; 2.A.53.3.3; the sulfate permease (sulp) family.
DR EnsemblBacteria; ACB00349; ACB00349; SYNPCC7002_A2371.
DR KEGG; syp:SYNPCC7002_A2371; -.
DR eggNOG; COG0659; Bacteria.
DR HOGENOM; CLU_003182_13_1_3; -.
DR OMA; VTNKFPI; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Metal-binding;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..566
FT /note="Bicarbonate transporter BicA"
FT /id="PRO_0000421878"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..42
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..93
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..169
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..247
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 436..546
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT BINDING 69
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q55415"
FT BINDING 262
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q55415"
FT BINDING 266
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q55415"
FT BINDING 304
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q55415"
FT BINDING 305
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q55415"
FT BINDING 306
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q55415"
SQ SEQUENCE 566 AA; 59605 MW; B3162BE1AF74D22D CRC64;
MQITNKIHFR NIRGDIFGGL TAAVIALPMA LAFGVASGAG AEAGLWGAVL VGFFAALFGG
TPTLISEPTG PMTVVMTAVI AHFTASAATP EEGLAIAFTV VMMAGVFQII FGSLKLGKYV
TMMPYTVISG FMSGIGIILV ILQLAPFLGQ ASPGGGVIGT LQNLPTLLSN IQPGETALAL
GTVAIIWFMP EKFKKVIPPQ LVALVLGTVI AFFVFPPEVS DLRRIGEIRA GFPELVRPSF
SPVEFQRMIL DAAVLGMLGC IDALLTSVVA DSLTRTEHNS NKELIGQGLG NLFSGLFGGI
AGAGATMGTV VNIQSGGRTA LSGLVRAFVL LVVILGAASL TATIPLAVLA GIAFKVGVDI
IDWSFLKRAH EISPKGALIM YGVILLTVLV DLIVAVGVGV FVANVLTIER MSNLQSEKVQ
TVSDADDNIR LTTTEKRWLD EGQGRVLLFQ LSGPMIFGVA KAIAREHNAM GDCDALVFDI
GEVPHMGVTA SLALENAIEE ALDKERQVYI VGAAGQTRRR LEKLKLFKRV PPDKCLMSRE
EALKNAVLGI YPHLADGVTA PSSEMG
