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NRTA_NOSS1
ID   NRTA_NOSS1              Reviewed;         440 AA.
AC   Q44292; O06469;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Nitrate/nitrite binding protein NrtA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=nrtA; OrderedLocusNames=alr0608;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8990301; DOI=10.1128/jb.179.2.477-486.1997;
RA   Frias J.E., Flores E., Herrero A.;
RT   "Nitrate assimilation gene cluster from the heterocyst-forming
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   J. Bacteriol. 179:477-486(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Frias J.E.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
RX   PubMed=8982006; DOI=10.1128/jb.179.1.258-266.1997;
RA   Cai Y., Wolk C.P.;
RT   "Nitrogen deprivation of Anabaena sp. strain PCC 7120 elicits rapid
RT   activation of a gene cluster that is essential for uptake and utilization
RT   of nitrate.";
RL   J. Bacteriol. 179:258-266(1997).
CC   -!- FUNCTION: Part of the ABC transporter complex NrtABCD involved in
CC       nitrate uptake. The complex is probably also involved in nitrite
CC       transport. NrtA is the substrate-binding protein.
CC       {ECO:0000250|UniProtKB:P38043}.
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:0000250|UniProtKB:P38043}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P38043}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38043}; Periplasmic side
CC       {ECO:0000250|UniProtKB:P38043}.
CC   -!- SIMILARITY: Belongs to the CmpA/NrtA family. {ECO:0000305}.
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DR   EMBL; X99709; CAA68041.2; -; Genomic_DNA.
DR   EMBL; BA000019; BAB72566.1; -; Genomic_DNA.
DR   EMBL; U61496; AAC46075.1; -; Genomic_DNA.
DR   PIR; AG1882; AG1882.
DR   RefSeq; WP_010994784.1; NZ_RSCN01000009.1.
DR   AlphaFoldDB; Q44292; -.
DR   SMR; Q44292; -.
DR   STRING; 103690.17129954; -.
DR   TCDB; 3.A.1.16.4; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; BAB72566; BAB72566; BAB72566.
DR   KEGG; ana:alr0608; -.
DR   eggNOG; COG0715; Bacteria.
DR   OMA; GPKKDMA; -.
DR   OrthoDB; 1832232at2; -.
DR   Proteomes; UP000002483; Chromosome.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion transport; Lipoprotein; Membrane;
KW   Nitrate assimilation; Palmitate; Reference proteome; Signal; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..440
FT                   /note="Nitrate/nitrite binding protein NrtA"
FT                   /id="PRO_0000057955"
FT   REGION          30..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100
FT                   /ligand="nitrate"
FT                   /ligand_id="ChEBI:CHEBI:17632"
FT                   /evidence="ECO:0000250|UniProtKB:P73452"
FT   BINDING         148
FT                   /ligand="nitrate"
FT                   /ligand_id="ChEBI:CHEBI:17632"
FT                   /evidence="ECO:0000250|UniProtKB:P73452"
FT   BINDING         193
FT                   /ligand="nitrate"
FT                   /ligand_id="ChEBI:CHEBI:17632"
FT                   /evidence="ECO:0000250|UniProtKB:P73452"
FT   BINDING         237
FT                   /ligand="nitrate"
FT                   /ligand_id="ChEBI:CHEBI:17632"
FT                   /evidence="ECO:0000250|UniProtKB:P73452"
FT   BINDING         266
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:0000250|UniProtKB:P73452"
FT   LIPID           26
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P73452"
FT   CONFLICT        100
FT                   /note="W -> C (in Ref. 1; CAA68041)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   440 AA;  48476 MW;  29937A41FB45CE9C CRC64;
     MTHVSRRKFL FTTGAAAAAS ILVHGCTSNG SQSATTGEQA PSAAPAANVS AANAPKVETT
     KAKLGFIPLT DAAPLIIAKE KGFFAKYGMT DIEVIKQKSW PVTRDNLKIG SSGGGIDGAH
     ILSPMPYLMT INDKVPMYIL ARLNTNGQAI SVAEKFKELN VNLESKSLKD AAIKAKADKK
     ALKMGITFPG GTHDLWMRYW LAAGGINPDQ DVVLEAVPPP QMVANMKVNT VDGFCVGEPW
     NAQLVNQKIG YSALVTGELW KDHPEKAFSM RQDWIEQNPN AAQAILMAIL EAQQWCDKAE
     NKEEMCKICS DRKYFNVAAA DIIERAKGNI DYGDGRKEQN FAHRMKFWAD NASYPYKSHD
     IWFLTEDIRW GYLPKDTKVQ DIVNQVNKED LWKKAAKAIG VADAEIPASS SRGVETFFDG
     VKFDPEKPEE YLNSLKIKKV
 
 
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