NRTA_SYNE7
ID NRTA_SYNE7 Reviewed; 443 AA.
AC P38043; Q31NV0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Nitrate/nitrite binding protein NrtA {ECO:0000305};
DE Flags: Precursor;
GN Name=nrtA {ECO:0000303|Ref.1}; OrderedLocusNames=Synpcc7942_1239;
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].
RC STRAIN=PCC 7942 / FACHB-805;
RA Omata T.;
RT "Cloning and characterization of the nrtA gene that encodes a 45-kDa
RT protein involved in nitrate transport in the cyanobacterium Synechococcus
RT PCC 7942.";
RL Plant Cell Physiol. 32:151-157(1991).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-443, AND FUNCTION.
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 [4]
RP PROTEIN SEQUENCE OF 251-263 AND 400-405, AND SUBUNIT.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=11032247; DOI=10.1080/15216540050167070;
RA Fresneau C., Zinovieva M., Blanot D., Batelier G., Arrio B.;
RT "The nitrogen source-dependent 126-kDa protein from Synechococcus PCC 7942
RT plasmalemma: a trimer of the NrtA nitrate-binding protein.";
RL IUBMB Life 49:527-532(2000).
RN [5]
RP FUNCTION IN NITRATE TRANSPORT, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16594065; DOI=10.1073/pnas.86.17.6612;
RA Omata T., Ohmori M., Arai N., Ogawa T.;
RT "Genetically engineered mutant of the cyanobacterium Synechococcus PCC 7942
RT defective in nitrate transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6612-6616(1989).
RN [6]
RP FUNCTION, 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=9006953; DOI=10.1074/jbc.272.5.3036;
RA Maeda S., Omata T.;
RT "Substrate-binding lipoprotein of the cyanobacterium Synechococcus sp.
RT strain PCC 7942 involved in the transport of nitrate and nitrite.";
RL J. Biol. Chem. 272:3036-3041(1997).
CC -!- FUNCTION: Part of the ABC transporter complex NrtABCD involved in
CC nitrate uptake (PubMed:16594065, PubMed:8437564, PubMed:7767600). The
CC complex is probably also involved in nitrite transport
CC (PubMed:7767600). NrtA is the substrate-binding protein
CC (PubMed:8437564, PubMed:7767600, PubMed:9006953). Binds both nitrate
CC and nitrite with high affinity (PubMed:9006953).
CC {ECO:0000269|PubMed:16594065, ECO:0000269|PubMed:7767600,
CC ECO:0000269|PubMed:8437564, ECO:0000269|PubMed:9006953}.
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) (PubMed:7767600). NrtA can form homotrimers (PubMed:11032247).
CC {ECO:0000269|PubMed:11032247, ECO:0000305|PubMed:7767600}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16594065,
CC ECO:0000305|PubMed:7767600}; Lipid-anchor {ECO:0000269|PubMed:9006953,
CC ECO:0000305|PubMed:7767600}; Periplasmic side
CC {ECO:0000305|PubMed:7767600}.
CC -!- INDUCTION: By nitrate, when present in the medium as source of
CC nitrogen. Expression is suppressed by ammonium.
CC {ECO:0000269|PubMed:16594065}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not grow under low concentrations of
CC nitrate (PubMed:16594065). Mutant is totally defective in nitrate
CC uptake but shows significant nitrite uptake (PubMed:9006953).
CC {ECO:0000269|PubMed:16594065, ECO:0000269|PubMed:9006953}.
CC -!- SIMILARITY: Belongs to the CmpA/NrtA family. {ECO:0000305}.
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DR EMBL; D12723; BAA02218.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57269.1; -; Genomic_DNA.
DR EMBL; X61625; CAA43809.1; -; Genomic_DNA.
DR RefSeq; WP_011242625.1; NC_007604.1.
DR AlphaFoldDB; P38043; -.
DR SMR; P38043; -.
DR STRING; 1140.Synpcc7942_1239; -.
DR TCDB; 3.A.1.16.1; the atp-binding cassette (abc) superfamily.
DR PRIDE; P38043; -.
DR EnsemblBacteria; ABB57269; ABB57269; Synpcc7942_1239.
DR KEGG; syf:Synpcc7942_1239; -.
DR eggNOG; COG0715; Bacteria.
DR HOGENOM; CLU_037398_3_0_3; -.
DR OMA; GPKKDMA; -.
DR OrthoDB; 1832232at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1239-MON; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd13553; PBP2_NrtA_CpmA_like; 1.
DR InterPro; IPR044527; NrtA/CpmA_ABC-bd_dom.
DR InterPro; IPR006311; TAT_signal.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Ion transport; Lipoprotein; Membrane; Nitrate assimilation; Palmitate;
KW Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..443
FT /note="Nitrate/nitrite binding protein NrtA"
FT /id="PRO_0000057956"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000250|UniProtKB:P73452"
FT BINDING 150
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000250|UniProtKB:P73452"
FT BINDING 195
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000250|UniProtKB:P73452"
FT BINDING 239
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000250|UniProtKB:P73452"
FT BINDING 268
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000250|UniProtKB:P73452"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="E -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 48425 MW; 2CE1987B15406705 CRC64;
MSQFSRRKFL LTAGGTAAAA LWLNACGSNN SSTDTTGSTS TPAPSGTSGG DAPEVKGVTL
GFIALTDAAP VIIALEKGLF AKYGLPDTKV VKQTSWAVTR DNLELGSDRG GIDGAHILSP
MPYLLTAGTI TKSQKPLPMY ILARLNTQGQ GISLSNEFLA EKVQIKDPKL KAIADQKKAS
GKLLKAAVTF PGGTHDLWMR YWLAANGIDP NNDADLVVIP PPQMVANMQT GTMDTFCVGE
PWNARLVNKK LGYTAAVTGE LWKFHPEKAL TIRADWADKN PKATMALLKA VQEAQIWCED
PANLDELCQI TAQDKYFKTS VEDIKPRLQG DIDYGDGRSV KNSDLRMRFW SENASFPYKS
HDLWFLTEDI RWGYLPASTD TKALIEKVNR SDLWREAAKA IGREQDIPAS DSRGVETFFD
GVTFDPENPQ AYLDGLKFKA IKA
