ID   NRTD_SYNE7              Reviewed;         274 AA.
AC   P38046; Q31NV3;
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 NrtD {ECO:0000305};
DE            EC=7.3.2.4 {ECO:0000305|PubMed:7767600};
GN   Name=nrtD {ECO:0000303|PubMed:8437564}; OrderedLocusNames=Synpcc7942_1236;
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, AND DISRUPTION 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).
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   -!- 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   -!- DISRUPTION PHENOTYPE: Mutant requires high concentration of nitrate for
CC       growth. It grows normally with nitrite or ammonium as the nitrogen
CC       source. {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; CAA43812.1; -; Genomic_DNA.
DR   EMBL; X74597; CAA52674.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57266.1; -; Genomic_DNA.
DR   RefSeq; WP_011242628.1; NC_007604.1.
DR   AlphaFoldDB; P38046; -.
DR   SMR; P38046; -.
DR   STRING; 1140.Synpcc7942_1236; -.
DR   TCDB; 3.A.1.16.1; the atp-binding cassette (abc) superfamily.
DR   PRIDE; P38046; -.
DR   EnsemblBacteria; ABB57266; ABB57266; Synpcc7942_1236.
DR   KEGG; syf:Synpcc7942_1236; -.
DR   eggNOG; COG1116; Bacteria.
DR   HOGENOM; CLU_000604_1_22_3; -.
DR   OMA; AFIETRE; -.
DR   OrthoDB; 1832232at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1236-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   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; 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..274
FT                   /note="Nitrate import ATP-binding protein NrtD"
FT                   /id="PRO_0000092648"
FT   DOMAIN          17..250
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   274 AA;  30366 MW;  7963193472ABE49B CRC64;
     MTAILPSTAA TVNTGFLHFD CVGKTFPTPR GPYVAIEDVN LSVQQGEFIC VIGHSGCGKS
     TLLNLVSGFS QPTSGGVYLD GQPIQEPGPD RMVVFQNYSL LPWKSARDNI ALAVKAARPH
     LSTSEQRQVV DHHLELVGLT EAQHKRPDQL SGGMKQRVAI ARALSIRPEV LILDEPFGAL
     DAITKEELQE ELLNIWEEAR PTVLMITHDI DEALFLADRV VMMTNGPAAT IGEVLEIPFD
     RPREREAVVE DPRYAQLRTE ALDFLYRRFA HDDD