GLNH_ECOLI
ID GLNH_ECOLI Reviewed; 248 AA.
AC P0AEQ3; P10344;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glutamine-binding periplasmic protein;
DE Short=GlnBP;
DE Flags: Precursor;
GN Name=glnH; OrderedLocusNames=b0811, JW0796;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-32, FUNCTION,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=3027504; DOI=10.1007/bf00430437;
RA Nohno T., Saito T., Hong J.;
RT "Cloning and complete nucleotide sequence of the Escherichia coli glutamine
RT permease operon (glnHPQ).";
RL Mol. Gen. Genet. 205:260-269(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 23-34.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=8831790; DOI=10.1006/jmbi.1996.0509;
RA Hsiao C.-D., Sun Y.-J., Rose J., Wang B.-C.;
RT "The crystal structure of glutamine-binding protein from Escherichia
RT coli.";
RL J. Mol. Biol. 262:225-242(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
RX PubMed=9571045; DOI=10.1006/jmbi.1998.1675;
RA Sun Y.-J., Rose J., Wang B.-C., Hsiao C.-D.;
RT "The structure of glutamine-binding protein complexed with glutamine at
RT 1.94-A resolution: comparisons with other amino acid binding proteins.";
RL J. Mol. Biol. 278:219-229(1998).
CC -!- FUNCTION: Involved in a glutamine-transport system GlnHPQ.
CC {ECO:0000269|PubMed:3027504}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:3027504}.
CC -!- INDUCTION: By lack of glutamine. {ECO:0000269|PubMed:3027504}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; X14180; CAA32382.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73898.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35483.1; -; Genomic_DNA.
DR PIR; S03181; JKECQ.
DR RefSeq; NP_415332.1; NC_000913.3.
DR RefSeq; WP_000843866.1; NZ_STEB01000019.1.
DR PDB; 1GGG; X-ray; 2.30 A; A/B=23-248.
DR PDB; 1WDN; X-ray; 1.94 A; A=23-248.
DR PDBsum; 1GGG; -.
DR PDBsum; 1WDN; -.
DR AlphaFoldDB; P0AEQ3; -.
DR BMRB; P0AEQ3; -.
DR SASBDB; P0AEQ3; -.
DR SMR; P0AEQ3; -.
DR BioGRID; 4259974; 30.
DR ComplexPortal; CPX-4822; Glutamine ABC transporter complex.
DR IntAct; P0AEQ3; 1.
DR STRING; 511145.b0811; -.
DR TCDB; 3.A.1.3.2; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AEQ3; -.
DR jPOST; P0AEQ3; -.
DR PaxDb; P0AEQ3; -.
DR PRIDE; P0AEQ3; -.
DR EnsemblBacteria; AAC73898; AAC73898; b0811.
DR EnsemblBacteria; BAA35483; BAA35483; BAA35483.
DR GeneID; 66670917; -.
DR GeneID; 944872; -.
DR KEGG; ecj:JW0796; -.
DR KEGG; eco:b0811; -.
DR PATRIC; fig|1411691.4.peg.1467; -.
DR EchoBASE; EB0381; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_2_6; -.
DR InParanoid; P0AEQ3; -.
DR OMA; IFATYSI; -.
DR PhylomeDB; P0AEQ3; -.
DR BioCyc; EcoCyc:GLNH-MON; -.
DR BioCyc; MetaCyc:GLNH-MON; -.
DR EvolutionaryTrace; P0AEQ3; -.
DR PRO; PR:P0AEQ3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:1903803; P:L-glutamine import across plasma membrane; IC:ComplexPortal.
DR CDD; cd00994; PBP2_GlnH; 1.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR044132; PBP2_GlnH.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR SMART; SM00079; PBPe; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Direct protein sequencing; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3027504,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 23..248
FT /note="Glutamine-binding periplasmic protein"
FT /id="PRO_0000031757"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:1WDN"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1WDN"
FT TURN 127..131
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:1WDN"
FT TURN 189..194
FT /evidence="ECO:0007829|PDB:1WDN"
FT STRAND 195..211
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:1WDN"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:1WDN"
SQ SEQUENCE 248 AA; 27190 MW; 89753157765D4384 CRC64;
MKSVLKVSLA ALTLAFAVSS HAADKKLVVA TDTAFVPFEF KQGDKYVGFD VDLWAAIAKE
LKLDYELKPM DFSGIIPALQ TKNVDLALAG ITITDERKKA IDFSDGYYKS GLLVMVKANN
NDVKSVKDLD GKVVAVKSGT GSVDYAKANI KTKDLRQFPN IDNAYMELGT NRADAVLHDT
PNILYFIKTA GNGQFKAVGD SLEAQQYGIA FPKGSDELRD KVNGALKTLR ENGTYNEIYK
KWFGTEPK
