BICA_SYNY3
ID BICA_SYNY3 Reviewed; 564 AA.
AC Q55415;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Bicarbonate transporter BicA {ECO:0000303|PubMed:31712753};
GN Name=bicA {ECO:0000303|PubMed:31712753};
GN OrderedLocusNames=sll0834 {ECO:0000312|EMBL:BAA10512.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF2-393 AND 409-564 IN COMPLEX WITH
RP BICARBONATE, FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND MUTAGENESIS OF THR-69; ASP-258; THR-262; THR-302; ALA-471; LEU-476;
RP ALA-486 AND LEU-490.
RX PubMed=31712753; DOI=10.1038/s41477-019-0538-1;
RA Wang C., Sun B., Zhang X., Huang X., Zhang M., Guo H., Chen X., Huang F.,
RA Chen T., Mi H., Yu F., Liu L.N., Zhang P.;
RT "Structural mechanism of the active bicarbonate transporter from
RT cyanobacteria.";
RL Nat. Plants 5:1184-1193(2019).
CC -!- FUNCTION: Low affinity, high-flux Na(+)-dependent bicarbonate
CC transporter (PubMed:31712753). Involved in carbone dioxide-
CC concentrating mechanisms (CCMs) that accumulate CO(2) and improve
CC photosynthetic carbon fixation (PubMed:31712753).
CC {ECO:0000269|PubMed:31712753}.
CC -!- SUBUNIT: Forms homodimers through the STAS cytoplasmic domain.
CC {ECO:0000269|PubMed:31712753}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:31712753}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:31712753}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA10512.1; -; Genomic_DNA.
DR PIR; S75777; S75777.
DR PDB; 6KI1; X-ray; 2.81 A; A/B=2-393.
DR PDB; 6KI2; X-ray; 2.20 A; A/B=409-564.
DR PDBsum; 6KI1; -.
DR PDBsum; 6KI2; -.
DR AlphaFoldDB; Q55415; -.
DR SMR; Q55415; -.
DR STRING; 1148.1001268; -.
DR PaxDb; Q55415; -.
DR EnsemblBacteria; BAA10512; BAA10512; BAA10512.
DR KEGG; syn:sll0834; -.
DR eggNOG; COG0659; Bacteria.
DR InParanoid; Q55415; -.
DR OMA; VTNKFPI; -.
DR PhylomeDB; Q55415; -.
DR Proteomes; UP000001425; 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:0015138; F:fumarate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IBA:GO_Central.
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:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015741; P:fumarate transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
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 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Metal-binding; Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..564
FT /note="Bicarbonate transporter BicA"
FT /id="PRO_0000449604"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 38..40
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 41..58
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 59..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 71..86
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 87..90
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 91..112
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 113..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 146..170
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 171..185
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 186..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 197..211
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 212..240
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 241..269
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 270..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 276..292
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 293..302
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 303..312
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 313..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 339..341
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 342..357
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 358..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 391..392
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TRANSMEM 393..405
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31712753"
FT TOPO_DOM 406..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31712753"
FT DOMAIN 432..542
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:0000269|PubMed:31712753,
FT ECO:0007744|PDB:6KI1"
FT BINDING 258
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:31712753,
FT ECO:0007744|PDB:6KI1"
FT BINDING 262
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:31712753,
FT ECO:0007744|PDB:6KI1"
FT BINDING 300
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:31712753,
FT ECO:0007744|PDB:6KI1"
FT BINDING 301
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:31712753,
FT ECO:0007744|PDB:6KI1"
FT BINDING 302
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:31712753,
FT ECO:0007744|PDB:6KI1"
FT MUTAGEN 69
FT /note="T->A: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT MUTAGEN 258
FT /note="D->A,E: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT MUTAGEN 262
FT /note="T->A: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT MUTAGEN 302
FT /note="T->A: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT MUTAGEN 471
FT /note="A->N: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT MUTAGEN 476
FT /note="L->S: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT MUTAGEN 486
FT /note="A->E: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT MUTAGEN 490
FT /note="L->Q: Alters bicarbonate transport."
FT /evidence="ECO:0000269|PubMed:31712753"
FT HELIX 12..37
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:6KI1"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 123..146
FT /evidence="ECO:0007829|PDB:6KI1"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 241..268
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:6KI1"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 316..337
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:6KI1"
FT HELIX 370..390
FT /evidence="ECO:0007829|PDB:6KI1"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6KI2"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 429..437
FT /evidence="ECO:0007829|PDB:6KI2"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:6KI2"
FT STRAND 441..449
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 455..466
FT /evidence="ECO:0007829|PDB:6KI2"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 484..500
FT /evidence="ECO:0007829|PDB:6KI2"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 511..519
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:6KI2"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:6KI2"
FT HELIX 535..544
FT /evidence="ECO:0007829|PDB:6KI2"
SQ SEQUENCE 564 AA; 59049 MW; 25A7330C730D5E4C CRC64;
MQITNKIHFR NLQGDLFGGV TAAVIALPMA LAFGIASGAG ATAGLWGAVI VGFFAALFGG
TPTLISEPTG PMTVVQTAVI ASLVAADPDN GLAMAFTVVM MAGLFQIAFG LLKLGKYVTM
MPYTVISGFM SGIGIILVIL QLAPFLGQAS PKGGVIGTLQ ALPNLVSNVR PVETLLALMT
VGIIWFMPSR WKKFAPPQLV ALVLGTIISI TLFGDLDIRR IGEIQAGLPA LQLPVFQADQ
LQRMLIDAAV LGMLGCIDAL LTSVVADSLT RTEHNSNKEL VGQGIGNVMS GLFGGLGGAG
ATMGTVVNIQ SGGRTALSGL IRAMVLLVVI LGAAKLAATI PLAVLAGIAF KVGVDIIDWG
FLKRAHHVSI KGALIMYAVI VLTVLVDLIA AVGIGVFIAN ILTIDRMSAL QSKAVKSISD
ADDEILLSAN EKRWLDEGNG RVLLFQLSGP MIFGVAKAIA REHNAIQECA AIVFDLSDVP
HLGVTASLAL ENAIEEAAEK GRAVYIVGAT GQTKRRLEKL QVFRFVPESN CYDDRSEALK
DAVLALGPHE SEDSPSSSSV QTTY
