CMPA_SYNY3
ID CMPA_SYNY3 Reviewed; 452 AA.
AC Q55460;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Bicarbonate-binding protein CmpA;
DE Flags: Precursor;
GN Name=cmpA; OrderedLocusNames=slr0040;
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 REGULATION BY CMPR.
RX PubMed=11222586; DOI=10.1128/jb.183.6.1891-1898.2001;
RA Omata T., Gohta S., Takahashi Y., Harano Y., Maeda S.;
RT "Involvement of a CbbR homolog in low CO2-induced activation of the
RT bicarbonate transporter operon in cyanobacteria.";
RL J. Bacteriol. 183:1891-1898(2001).
CC -!- FUNCTION: Part of the ABC transporter complex CmpABCD involved in
CC bicarbonate transport. Binds bicarbonate with high affinity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (CmpC and
CC CmpD), a transmembrane protein (CmpB) and a solute-binding protein
CC (CmpA). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: By carbon dioxide-limited conditions, probably via CmpR.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the CmpA/NrtA family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10803.1; -; Genomic_DNA.
DR PIR; S75956; S75956.
DR PDB; 2I48; X-ray; 1.60 A; A=27-452.
DR PDB; 2I49; X-ray; 1.35 A; A=27-452.
DR PDB; 2I4B; X-ray; 1.35 A; A=27-452.
DR PDB; 2I4C; X-ray; 1.70 A; A=27-452.
DR PDBsum; 2I48; -.
DR PDBsum; 2I49; -.
DR PDBsum; 2I4B; -.
DR PDBsum; 2I4C; -.
DR AlphaFoldDB; Q55460; -.
DR SMR; Q55460; -.
DR IntAct; Q55460; 1.
DR STRING; 1148.1001316; -.
DR PaxDb; Q55460; -.
DR EnsemblBacteria; BAA10803; BAA10803; BAA10803.
DR KEGG; syn:slr0040; -.
DR eggNOG; COG0715; Bacteria.
DR InParanoid; Q55460; -.
DR OMA; GGQWQMP; -.
DR PhylomeDB; Q55460; -.
DR EvolutionaryTrace; Q55460; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR CDD; cd13553; PBP2_NrtA_CpmA_like; 1.
DR InterPro; IPR044527; NrtA/CpmA_ABC-bd_dom.
DR InterPro; IPR006311; TAT_signal.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..35
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 36..452
FT /note="Bicarbonate-binding protein CmpA"
FT /id="PRO_0000341964"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:2I49"
FT TURN 130..136
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2I49"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:2I49"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 284..301
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:2I49"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 366..378
FT /evidence="ECO:0007829|PDB:2I49"
FT TURN 379..385
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:2I49"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2I49"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:2I49"
SQ SEQUENCE 452 AA; 49461 MW; B31E2F32CEF90447 CRC64;
MGSFNRRKFL LTSAATATGA LFLKGCAGNP PDPNAASTGT NPSPQAAGDI SPEMMPETAN
IKLGYIPIVE AAPLIIAQEK GFFAKYGMTG VEVSKQANWA SARDNVTIGS QGGGIDGGQW
QMPMPHLITE GIITNGNKVP MYVLAQLITQ GNGIAVAPMH EGKGVNLDIT KAADYIKGFN
KTNGRKFKAA HTFPNVNQDF WIRYWFAAGG VDPDTDIDLL AVPPAETVQG MRNGTMDAFS
TGDPWPYRIV TENIGYMAGL TAQIWPYHPE EYLAIRADWV DKNPKATKAL LKGIMEAQQW
IDDPKNRPEV VQIVSGRNYF NVPTTILESP FKGQYTMGDG QPAIDDFQKG PLYWKDGIGN
VSYPYKSHDL WFLTESIRWG FHKNAIPDLD TAQKIIDKVN REDLWREAAT EAGFTADIPS
STSRGVETFF DGITFDPANP SAYLQSLAIK KV
