ID CMPA_SYNE7 Reviewed; 450 AA.
AC P39660; Q31N51; Q55109;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Bicarbonate-binding protein CmpA;
DE Flags: Precursor;
GN Name=cmpA; Synonyms=cbpA; OrderedLocusNames=Synpcc7942_1488;
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=2498292; DOI=10.1128/jb.171.6.3486-3493.1989;
RA Reddy K.J., Masamoto K., Sherman D.M., Sherman L.A.;
RT "DNA sequence and regulation of the gene (cbpA) encoding the 42-kilodalton
RT cytoplasmic membrane carotenoprotein of the cyanobacterium Synechococcus
RT sp. strain PCC 7942.";
RL J. Bacteriol. 171:3486-3493(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 438-443, AND
RP INDUCTION.
RX PubMed=16667451; DOI=10.1104/pp.93.1.305;
RA Omata T., Carlson T.J., Ogawa T., Pierce J.;
RT "Sequencing and modification of the gene encoding the 42-kilodalton protein
RT in the cytoplasmic membrane of Synechococcus PCC 7942.";
RL Plant Physiol. 93:305-311(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION IN BICARBONATE TRANSPORT, AND INDUCTION.
RX PubMed=10557362; DOI=10.1073/pnas.96.23.13571;
RA Omata T., Price G.D., Badger M.R., Okamura M., Gohta S., Ogawa T.;
RT "Identification of an ATP-binding cassette transporter involved in
RT bicarbonate uptake in the cyanobacterium Synechococcus sp. strain PCC
RT 7942.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13571-13576(1999).
RN [5]
RP BINDING TO BICARBONATE.
RX PubMed=10779519; DOI=10.1074/jbc.m003034200;
RA Maeda S., Price G.D., Badger M.R., Enomoto C., Omata T.;
RT "Bicarbonate binding activity of the CmpA protein of the cyanobacterium
RT Synechococcus sp. strain PCC 7942 involved in active transport of
RT bicarbonate.";
RL J. Biol. Chem. 275:20551-20555(2000).
RN [6]
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.
CC {ECO:0000269|PubMed:10557362}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2498292};
CC Peripheral membrane protein {ECO:0000269|PubMed:2498292}.
CC -!- INDUCTION: By carbon dioxide-limited conditions, probably via CmpR.
CC Also induced by growth under high light intensities. Repressed by iron-
CC deficient conditions. {ECO:0000269|PubMed:10557362,
CC ECO:0000269|PubMed:16667451, ECO:0000269|PubMed:2498292}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CmpA/NrtA family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a carotenoid-binding protein.
CC {ECO:0000305|PubMed:2498292}.
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DR EMBL; M27055; AAA27303.1; -; Genomic_DNA.
DR EMBL; M32999; AAA03704.1; -; Unassigned_DNA.
DR EMBL; CP000100; ABB57518.1; -; Genomic_DNA.
DR RefSeq; WP_011378052.1; NZ_JACJTX010000004.1.
DR AlphaFoldDB; P39660; -.
DR SMR; P39660; -.
DR STRING; 1140.Synpcc7942_1488; -.
DR TCDB; 3.A.1.16.3; the atp-binding cassette (abc) superfamily.
DR PaxDb; 1140-Synpcc7942_1488; -.
DR GeneID; 76400228; -.
DR KEGG; syf:Synpcc7942_1488; -.
DR eggNOG; COG0715; Bacteria.
DR HOGENOM; CLU_037398_3_0_3; -.
DR OrthoDB; 568193at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1488-MONOMER; -.
DR Proteomes; UP000889800; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:CACAO.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd13553; PBP2_NrtA_CpmA_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR044527; NrtA/CpmA_ABC-bd_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR30024; ALIPHATIC SULFONATES-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR30024:SF7; NITRATE_NITRITE BINDING PROTEIN NRTA; 1.
DR Pfam; PF13379; NMT1_2; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Ion transport; Membrane; Reference proteome; Signal; Transport.
FT SIGNAL 1..36
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 37..450
FT /note="Bicarbonate-binding protein CmpA"
FT /id="PRO_0000020847"
FT CONFLICT 119
FT /note="M -> I (in Ref. 1; AAA27303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 49108 MW; EF2B5C734BCD2817 CRC64;
MNEFQPVNRR QFLFTLGATA ASAILLKGCG NPPSSSGGGT SSTTQPTAAG ASDLEVKTIK
LGYIPIFEAA PLIIGREKGF FAKYGLDVEV SKQASWAAAR DNVILGSAGG GIDGGQWQMP
MPALLTEGAI SNGQKVPMYV LACLSTQGNG IAVSNQLKAQ NLGLKLAPNR DFILNYPQTS
GRKFKASYTF PNANQDFWIR YWFAAGGIDP DKDIELLTVP SAETLQNMRN GTIDCFSTGD
PWPSRIAKDD IGYQAALTGQ MWPYHPEEFL ALRADWVDKH PKATLALLMG LMEAQQWCDQ
KANRAEMAKI LSGRNFFNVP VSILQPILEG QIKVGADGKD LNNFDAGPLF WKSPRGSVSY
PYKGLTLWFL VESIRWGFNK QVLPDIAAAQ KLNDRVTRED LWQEAAKKLG VPAADIPTGS
TRGTETFFDG ITYNPDSPQA YLQSLKIKRA
//
