P0A9Z1 (GLNB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nitrogen regulatory protein P-II 1

Gene names

Name:	glnB
Ordered Locus Names:	b2553, JW2537

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	112 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by glnE, so activating the enzyme.
Subunit structure	Homotrimer. Ref.10
Post-translational modification	Uridylylated/deuridylylated by glnD.
Sequence similarities	Belongs to the P(II) protein family.
Sequence caution	The sequence AAA23883.1 differs from that shown. Reason: Frameshift at positions 103 and 105.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Ligand	Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of nitrogen utilization Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	enzyme regulator activity Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
glnL	P0AFB5	4	EBI-551053,EBI-701156

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 112

112

Nitrogen regulatory protein P-II 1

PRO_0000139771

Amino acid modifications

Modified residue

51

1

O-UMP-tyrosine

Experimental info

Sequence conflict

19

1

A → R in AAA23883. Ref.1

Sequence conflict

81 – 82

2

AQ → E in AAA23883. Ref.1

Secondary structure

1

.

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112

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

10 – 12

3

Helix

13 – 23

11

Beta strand

28 – 37

10

Beta strand

56 – 65

10

Helix

67 – 69

3

Helix

70 – 81

12

Beta strand

90 – 95

6

Beta strand

97 – 101

5

Turn

102 – 104

3

Sequences

	Sequence		Length	Mass (Da)
	P0A9Z1 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: D1A4158A2F225042	FASTA	112	12,425
	10 20 30 40 50 60 MKKIDAIIKP FKLDDVREAL AEVGITGMTV TEVKGFGRQK GHTELYRGAE YMVDFLPKVK 70 80 90 100 110 IEIVVPDDIV DTCVDTIIRT AQTGKIGDGK IFVFDVARVI RIRTGEEDDA AI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene." Son H.S., Rhee S.G. J. Biol. Chem. 262:8690-8695(1987) [PubMed: 2885322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of the Klebsiella pneumoniae glnB gene: nucleotide sequence of wild-type and mutant alleles." Holtel A., Merrick M. Mol. Gen. Genet. 215:134-138(1988) [PubMed: 2907369] [Abstract] Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]	"Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12." Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E., Poole R.K. Mol. Gen. Genet. 226:49-58(1991) [PubMed: 2034230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"The glnB region of the Escherichia coli chromosome." Liu J., Magasanik B. J. Bacteriol. 175:7441-7449(1993) [PubMed: 8226691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli." van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D. Mol. Microbiol. 9:443-458(1993) [PubMed: 8412694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"Regulation of transcription of the glnALG operon of Escherichia coli by protein phosphorylation." Magasanik B. Biochimie 71:1005-1012(1989) [PubMed: 2574599] [Abstract] Cited for: REVIEW.
[10]	"Escherichia coli PII protein: purification, crystallization and oligomeric structure." Vasudevan S.G., Gedye C., Dixon N.E., Cheah E., Carr P.D., Suffolk P.M., Jeffrey P.D., Ollis D.L. FEBS Lett. 337:255-258(1994) [PubMed: 8293810] [Abstract] Cited for: CRYSTALLIZATION, SUBUNIT.
[11]	"Structure of the Escherichia coli signal transducing protein PII." Cheah E., Carr P.D., Suffolk P.M., Vasuvedan S.G., Dixon N.E., Ollis D.L. Structure 2:981-990(1994) [PubMed: 7866749] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[12]	"X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A." Carr P.D., Cheah E., Suffolk P.M., Vasudevan S.G., Dixon N.E., Ollis D.L. Acta Crystallogr. D 52:93-104(1996) [PubMed: 15299730] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16778 Genomic DNA. Translation: AAA23883.1. Frameshift.
X58872 Genomic DNA. Translation: CAA41683.1.
S67014 Genomic DNA. Translation: AAB28779.1.
U00096 Genomic DNA. Translation: AAC75606.1.
AP009048 Genomic DNA. Translation: BAA16461.1.
Z21843 Genomic DNA. Translation: CAA79890.1.

PIR

RGECP2. C49940.

RefSeq

NP_417048.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PIL	X-ray	2.70	A	1-112	[»]
2PII	X-ray	1.90	A	1-112	[»]

ProteinModelPortal

P0A9Z1.

SMR

P0A9Z1. Positions 1-112.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35005N.

IntAct

P0A9Z1. 19 interactions.

MINT

MINT-1235669.

2D gel databases

ECO2DBASE

F012.2. 6TH EDITION.

Proteomic databases

PRIDE

P0A9Z1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004144; EBESCP00000004144; EBESCG00000003383.
EBESCT00000004145; EBESCP00000004145; EBESCG00000003383.
EBESCT00000004146; EBESCP00000004146; EBESCG00000003383.
EBESCT00000014755; EBESCP00000014046; EBESCG00000013815.

GeneID

947016.

GenomeReviews

Gene locus JW2537 in contig AP009048_GR.
Gene locus b2553 in contig U00096_GR.

KEGG

ecj:JW2537.
eco:b2553.

PATRIC

32120505. VBIEscCol129921_2655.

Organism-specific databases

EchoBASE

EB0379.

EcoGene

EG10384. glnB.

Phylogenomic databases

eggNOG

COG0347.

GeneTree

EBGT00050000008988.

HOGENOM

HBG748089.

OMA

IERYRGN.

PhylomeDB

P0A9Z1.

ProtClustDB

PRK10858.

Enzyme and pathway databases

BioCyc

EcoCyc:PROTEIN-PII.

Gene expression databases

Genevestigator

P0A9Z1.

Family and domain databases

InterPro

IPR002187. N-reg_PII.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
IPR017918. N-reg_PII_CS.
IPR002332. N-reg_PII_urydylation_site.
[Graphical view]

Gene3D

G3DSA:3.30.70.120. PII_glnB. 1 hit.

KO

K04751.

Pfam

PF00543. P-II. 1 hit.
[Graphical view]

PRINTS

PR00340. PIIGLNB.

SMART

SM00938. P-II. 1 hit.
[Graphical view]

SUPFAM

SSF54913. N-reg_PII-like_a/b. 1 hit.

PROSITE

PS00638. PII_GLNB_CTER. 1 hit.
PS51343. PII_GLNB_DOM. 1 hit.
PS00496. PII_GLNB_UMP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLNB_ECOLI

Accession

Primary (citable) accession number: P0A9Z1
Secondary accession number(s): P05826

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program