ID   NRTC_SYNE7              Reviewed;         659 AA.
AC   P38045; Q31NV2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Nitrate import ATP-binding protein NrtC {ECO:0000305};
DE            EC=7.3.2.4 {ECO:0000305|PubMed:7767600};
GN   Name=nrtC {ECO:0000303|PubMed:8437564}; OrderedLocusNames=Synpcc7942_1237;
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], FUNCTION, DOMAIN, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=8437564; DOI=10.1007/bf00277112;
RA   Omata T., Andriesse X., Hirano A.;
RT   "Identification and characterization of a gene cluster involved in nitrate
RT   transport in the cyanobacterium Synechococcus sp. PCC7942.";
RL   Mol. Gen. Genet. 236:193-202(1993).
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, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=PCC 7942 / FACHB-805;
RX   PubMed=7767600; DOI=10.1093/oxfordjournals.pcp.a078751;
RA   Omata T.;
RT   "Structure, function and regulation of the nitrate transport system of the
RT   cyanobacterium Synechococcus sp. PCC7942.";
RL   Plant Cell Physiol. 36:207-213(1995).
RN   [4]
RP   ACTIVITY REGULATION, AND DOMAIN.
RX   PubMed=9341163; DOI=10.1074/jbc.272.43.27197;
RA   Kobayashi M., Rodriguez R., Lara C., Omata T.;
RT   "Involvement of the C-terminal domain of an ATP-binding subunit in the
RT   regulation of the ABC-type nitrate/nitrite transporter of the
RT   Cyanobacterium synechococcus sp. strain PCC 7942.";
RL   J. Biol. Chem. 272:27197-27201(1997).
CC   -!- FUNCTION: Part of the ABC transporter complex NrtABCD involved in
CC       nitrate uptake (PubMed:7767600, PubMed:8437564). The complex is
CC       probably also involved in nitrite transport (PubMed:7767600). Probably
CC       responsible for energy coupling to the transport system
CC       (PubMed:7767600). {ECO:0000269|PubMed:8437564,
CC       ECO:0000305|PubMed:7767600}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + nitrate(out) = ADP + H(+) + nitrate(in) +
CC         phosphate; Xref=Rhea:RHEA:13181, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17632, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.4;
CC         Evidence={ECO:0000305|PubMed:7767600};
CC   -!- ACTIVITY REGULATION: Transport is inhibited by ammonium. The C-terminal
CC       domain of NrtC is involved in the ammonium-promoted inhibition of the
CC       nitrate/nitrite transporter. {ECO:0000269|PubMed:9341163}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (NrtC and
CC       NrtD), two transmembrane proteins (NrtB) and a solute-binding protein
CC       (NrtA). {ECO:0000305|PubMed:7767600}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:7767600};
CC       Peripheral membrane protein {ECO:0000305|PubMed:7767600}; Cytoplasmic
CC       side {ECO:0000305|PubMed:7767600}.
CC   -!- DOMAIN: Contains an ATP-binding N-terminal domain and a NrtA-like C-
CC       terminal domain, which are connected by a segment containing an
CC       abundance of glutamine, alanine and positively charged amino acids
CC       (PubMed:8437564). The N-terminal domain is required for activity and
CC       the C-terminal domain is involved in regulation of the activity
CC       (PubMed:9341163). {ECO:0000269|PubMed:8437564,
CC       ECO:0000269|PubMed:9341163}.
CC   -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on nitrate, but grows
CC       normally with nitrite or ammonium as the nitrogen source.
CC       {ECO:0000269|PubMed:8437564}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Nitrate/nitrite/cyanate uptake transporter (NitT) (TC 3.A.1.16) family.
CC       {ECO:0000305}.
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DR   EMBL; X61625; CAA43811.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57267.1; -; Genomic_DNA.
DR   PIR; S30893; S30893.
DR   RefSeq; WP_011242627.1; NC_007604.1.
DR   AlphaFoldDB; P38045; -.
DR   SMR; P38045; -.
DR   STRING; 1140.Synpcc7942_1237; -.
DR   TCDB; 3.A.1.16.1; the atp-binding cassette (abc) superfamily.
DR   PRIDE; P38045; -.
DR   EnsemblBacteria; ABB57267; ABB57267; Synpcc7942_1237.
DR   KEGG; syf:Synpcc7942_1237; -.
DR   eggNOG; COG0715; Bacteria.
DR   eggNOG; COG1116; Bacteria.
DR   HOGENOM; CLU_025127_1_1_3; -.
DR   OrthoDB; 1832232at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1237-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015414; F:ABC-type nitrate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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   Nitrate assimilation; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..659
FT                   /note="Nitrate import ATP-binding protein NrtC"
FT                   /id="PRO_0000092646"
FT   DOMAIN          5..239
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          255..278
FT                   /note="Linker"
FT                   /evidence="ECO:0000305|PubMed:8437564"
FT   REGION          279..659
FT                   /note="NrtA-like"
FT                   /evidence="ECO:0000305|PubMed:8437564"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   659 AA;  72346 MW;  1D445792A5A76134 CRC64;
     MSVFLAVDHV HQVFDLPGGG QYIALKDVSL NIRPGEFISL IGHSGCGKST LLNLIAGLAQ
     PSSGGIILEG RQVTEPGPDR MVVFQNYSLL PWRTVRQNIA LAVDSVLHDR NRTERRTIIE
     ETIDLVGLRA AADKYPHEIS GGMKQRVAIA RGLAIRPKLL LLDEPFGALD ALTRGNLQEQ
     LMRICQEAGV TAVMVTHDVD EALLLSDRVV MLTNGPAAQI GQILEVDFPR PRQRLEMMET
     PHYYDLRNEL INFLQQQRRA KRRAKAAAPA PAVAASQQKT VRLGFLPGND CAPLAIAQEL
     GLFQDLGLSV ELQSFLTWEA LEDSIRLGQL EGALMMAAQP LAMTMGLGGH RPFAIATPLT
     VSRNGGAIAL SRRYLNAGVR SLEDLCQFLA ATPQRLRLAI PDPIAMPALL LRYWLASAGL
     NPEQDVELVG MSPYEMVEAL KAGDIDGFAA GEMRIALAVQ AGAAYVLATD LDIWAGHPEK
     VLGLPEAWLQ VNPETAIALC SALLKAGELC DDPRQRDRIV EVLQQPQYLG SAAGTVLQRY
     FDFGLGDEPT QILRFNQFHV DQANYPNPLE GTWLLTQLCR WGLTPLPKNR QELLDRVYRR
     DIYEAAIAAV GFPLITPSQR GFELFDAVPF DPDSPLRYLE QFEIKAPIQV APIPLATSA