ID   CMPC_SYNE7              Reviewed;         663 AA.
AC   Q55107; Q31N49;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Bicarbonate transport ATP-binding protein CmpC;
DE            EC=7.6.2.-;
GN   Name=cmpC; OrderedLocusNames=Synpcc7942_1490;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Omata T.;
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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. Responsible for energy coupling to the transport
CC       system (Probable). {ECO:0000305|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:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By carbon dioxide-limited conditions, probably via CmpR.
CC       {ECO:0000269|PubMed:10557362}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Nitrate/nitrite/cyanate uptake transporter (NitT) (TC 3.A.1.16) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D26358; BAA05388.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57520.1; -; Genomic_DNA.
DR   RefSeq; WP_011244786.1; NC_007604.1.
DR   AlphaFoldDB; Q55107; -.
DR   SMR; Q55107; -.
DR   STRING; 1140.Synpcc7942_1490; -.
DR   TCDB; 3.A.1.16.3; the atp-binding cassette (abc) superfamily.
DR   PRIDE; Q55107; -.
DR   EnsemblBacteria; ABB57520; ABB57520; Synpcc7942_1490.
DR   KEGG; syf:Synpcc7942_1490; -.
DR   eggNOG; COG0715; Bacteria.
DR   eggNOG; COG1116; Bacteria.
DR   HOGENOM; CLU_025127_0_0_3; -.
DR   OMA; LTMTRNG; -.
DR   OrthoDB; 1832232at2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015112; F:nitrate transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd13553; PBP2_NrtA_CpmA_like; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005890; NO3_transporter_ATP-bd.
DR   InterPro; IPR044527; NrtA/CpmA_ABC-bd_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01184; ntrCD; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..663
FT                   /note="Bicarbonate transport ATP-binding protein CmpC"
FT                   /id="PRO_0000341954"
FT   DOMAIN          5..239
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          281..663
FT                   /note="CmpA-like"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   663 AA;  73492 MW;  C744FEF286BCB15A CRC64;
     MSLFVAVENI EKSFPLSGGN EYLALKGIDL EIKQGEFISL IGHSGCGKST LLNLIAGLEL
     PTDGAVSLEG QQITAPGPDR MVVFQNYSLF PWLTVRENIA LAVDEVLRDL PKEERQAIVE
     EHIQLVGLGH AADKPPAQLS GGMKQRVAIA RGLATRPKLL LLDEPFGALD ALTRGNLQEK
     LMQICEENHV TAVMVTHDVD EAVLLSDRIV MLTNGPGSKI GGILEVDIPR PRKRMDVVHH
     PSYYSLRSEI IYFLNQQKRV KKLNARKVTT VARHGLEKVN LEIGYVPLMA CAPLVVAQEK
     AFFAKHGLDE VSLVRETSWR GIVDGLTENY LDAAQMPAGM PVWMSVGGQG GSPLPIVSSL
     TMSRNGNGIT LSKALYDEGI QTVDDFRNLL RSTADKQHIM GIVHPASMHN LLLRYWLAAN
     QIDPDRDVQL RTIPPAQMVA DLKDGTIDGY CIGEPWNAWA AQKEIGFTIA SDLEIWNGHP
     GKVLGVREDW ANRYPNSHVA LVKALLEACQ YCEDPANWDE LRELLSDRRY LSCPKEYIQF
     SQSTADDLAV PHHRFAGAGV NRPSRTEHLW MMTQLARWGD VPFPRNWVEI LERVCRVGVF
     STAARELGLS EVVNYQRSTP VELFDGVPFN AEDPIAYLNS LPIHRDFSVA EIALDQPRPI
     AAA