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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
 
 
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