NRTA_SYNY3
ID NRTA_SYNY3 Reviewed; 446 AA.
AC P73452;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nitrate/nitrite binding protein NrtA {ECO:0000305};
DE Flags: Precursor;
GN Name=nrtA {ECO:0000303|PubMed:16777960}; OrderedLocusNames=sll1450;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2] {ECO:0007744|PDB:2G29}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 30-446 IN COMPLEX WITH NITRATE,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=16777960; DOI=10.1073/pnas.0602517103;
RA Koropatkin N.M., Pakrasi H.B., Smith T.J.;
RT "Atomic structure of a nitrate-binding protein crucial for photosynthetic
RT productivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9820-9825(2006).
CC -!- FUNCTION: Part of the ABC transporter complex NrtABCD involved in
CC nitrate uptake (PubMed:16777960). The complex is probably also involved
CC in nitrite transport (By similarity). NrtA is the substrate-binding
CC protein (PubMed:16777960). Binds nitrate (PubMed:16777960).
CC {ECO:0000250|UniProtKB:P38043, ECO:0000269|PubMed:16777960}.
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:16777960}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:16777960}; Lipid-anchor
CC {ECO:0000305|PubMed:16777960}; Periplasmic side
CC {ECO:0000305|PubMed:16777960}.
CC -!- DOMAIN: Composed of two domains (I and II) organized with a C-clamp
CC shape. {ECO:0000269|PubMed:16777960}.
CC -!- SIMILARITY: Belongs to the CmpA/NrtA family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17492.1; -; Genomic_DNA.
DR PIR; S77389; S77389.
DR PDB; 2G29; X-ray; 1.50 A; A=30-446.
DR PDBsum; 2G29; -.
DR AlphaFoldDB; P73452; -.
DR SMR; P73452; -.
DR STRING; 1148.1652571; -.
DR PaxDb; P73452; -.
DR EnsemblBacteria; BAA17492; BAA17492; BAA17492.
DR KEGG; syn:sll1450; -.
DR eggNOG; COG0715; Bacteria.
DR InParanoid; P73452; -.
DR OMA; GPKKDMA; -.
DR PhylomeDB; P73452; -.
DR EvolutionaryTrace; P73452; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR044527; NrtA/CpmA_ABC-bd_dom.
DR InterPro; IPR006311; TAT_signal.
DR SUPFAM; SSF54556; SSF54556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport;
KW Lipoprotein; Membrane; Nitrate assimilation; Palmitate; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..446
FT /note="Nitrate/nitrite binding protein NrtA"
FT /id="PRO_0000057957"
FT BINDING 102
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:16777960,
FT ECO:0007744|PDB:2G29"
FT BINDING 155
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:16777960,
FT ECO:0007744|PDB:2G29"
FT BINDING 196
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:16777960,
FT ECO:0007744|PDB:2G29"
FT BINDING 240
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:16777960,
FT ECO:0007744|PDB:2G29"
FT BINDING 269
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:16777960,
FT ECO:0007744|PDB:2G29"
FT LIPID 29
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:2G29"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 282..300
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:2G29"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2G29"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 361..373
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2G29"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2G29"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:2G29"
SQ SEQUENCE 446 AA; 48967 MW; 9C7196677AA181D0 CRC64;
MSNFSRSTRR KFMFTAGAAA IGGVVLHGCT SPTTTSTGTG TGSSTDQAIS PLVEGENAPE
VTTAKLGFIA LTDAAPLIIA KEKGFYAKYG MPDVEVLKQA SWGTTRDNLV LGSASGGIDG
AHILTPMPYL ITMGTVTDGK PTPMYILARL NVNGQGIQLG NNYKDLKVGT DAAPLKEAFA
KVTDPKVAMT FPGGTHDMWI RYWLAAGGME PGKDFSTIVV PPAQMVANVK VNAMESFCVG
EPWPLQTVNQ GVGYQALTTG QLWKDHPEKA FGMRADWVDQ NPKAAKALLM AVMEAQQWCD
QAENKEEMCQ ILSKREWFKV PFEDIIDRSK GIYNFGNGQE TFEDQEIMQK YWVDNASYPY
KSHDQWFLTE NIRWGYLPAS TDTKAIVDKV NREDLWREAA QALEVPADQI PSSPSRGIET
FFDGITFDPE NPQAYLDSLK IKSIKA
