P0AAP1 (ADRA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable diguanylate cyclase AdrA
Short name=DGC
EC=2.7.7.65

Gene names

Name:	adrA
Synonyms:	yaiC
Ordered Locus Names:	b0385, JW0376

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	A probable diguanylate cyclase. The last member of a cascade of expressed proteins, its expression requires YdaM. AdrA production induces biosynthesis of cellulose in some E.coli isolates, but not in K12 strains. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Ref.9
Catalytic activity	2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate. Ref.9
Cofactor	Binds 1 Mg2+ per monomer By similarity.
Pathway	Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
Subunit structure	Homodimer By similarity.
Subcellular location	Cell inner membrane; Multi-pass membrane protein Potential.
Induction	Expressed at 28 degrees Celsius in late stationary phase, more highly expressed on plates than in liquid medium. Expression is RpoS-, CsgD- and YdaM-dependent. Ref.6 Ref.7 Ref.8
Sequence similarities	Contains 1 GGDEF domain.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cyclic nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW diguanylate cyclase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorus-oxygen lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 371	371	Probable diguanylate cyclase AdrA		PRO_0000168588
Regions
	Transmembrane	46 – 66	21	Helical; Potential
	Transmembrane	68 – 88	21	Helical; Potential
	Transmembrane	112 – 132	21	Helical; Potential
	Transmembrane	143 – 163	21	Helical; Potential
	Transmembrane	171 – 191	21	Helical; Potential
	Domain	240 – 371	132	GGDEF
Sites
	Active site	291	1	Proton acceptor Potential
	Metal binding	248	1	Magnesium By similarity
	Metal binding	291	1	Magnesium By similarity
	Binding site	256	1	Substrate By similarity
	Binding site	265	1	Substrate By similarity
	Site	253	1	Transition state stabilizer Potential
Experimental info
	Mutagenesis	291 – 292	2	DE → AA: No c-di-GMP produced in an overexpressing strain. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P0AAP1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 1F5111C43481F32B	FASTA	371	41,537
	10 20 30 40 50 60 MFPKIMNDEN FFKKAAAHGE EPPLTPQNEH QRSGLRFARR VRLPRAVGLA GMFLPIASTL 70 80 90 100 110 120 VSHPPPGWWW LVLVGWAFVW PHLAWQIASR AVDPLSREIY NLKTDAVLAG MWVGVMGVNV 130 140 150 160 170 180 LPSTAMLMIM CLNLMGAGGP RLFVAGLVLM VVSCLVTLEL TGITVSFNSA PLEWWLSLPI 190 200 210 220 230 240 IVIYPLLFGW VSYQTATKLA EHKRRLQVMS TRDGMTGVYN RRHWETMLRN EFDNCRRHNR 250 260 270 280 290 300 DATLLIIDID HFKSINDTWG HDVGDEAIVA LTRQLQITLR GSDVIGRFGG DEFAVIMSGT 310 320 330 340 350 360 PAESAITAML RVHEGLNTLR LPNTPQVTLR ISVGVAPLNP QMSHYREWLK SADLALYKAK 370 KAGRNRTEVA A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"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.
[3]	"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.
[4]	"Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli." Chang C.N., Kuang W.-J., Chen E.Y. Gene 44:121-125(1986) [PubMed: 3533724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159. Strain: K12.
[5]	"The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix." Zogaj X., Nimtz M., Rohde M., Bokranz W., Roemling U. Mol. Microbiol. 39:1452-1463(2001) [PubMed: 11260463] [Abstract] Cited for: LACK OF CELLULOSE PRODUCTION IN K12 STRAINS. Strain: K12 / MC4100.
[6]	"Gene expression regulation by the Curli activator CsgD protein: modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion." Brombacher E., Baratto A., Dorel C., Landini P. J. Bacteriol. 188:2027-2037(2006) [PubMed: 16513732] [Abstract] Cited for: REGULATION BY CSGD. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli." Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R. Mol. Microbiol. 62:1014-1034(2006) [PubMed: 17010156] [Abstract] Cited for: INDUCTION, RPOS-DEPENDENCE, REGULATION CASCADE. Strain: K12 / MC4100.
[8]	"Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli." Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N., Hengge R. Microbiology 155:1318-1331(2009) [PubMed: 19332833] [Abstract] Cited for: INDUCTION, RPOS-DEPENDENCE. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole-cell assays suitable for high-throughput screening of biofilm inhibitors." Antoniani D., Bocci P., Maciag A., Raffaelli N., Landini P. Appl. Microbiol. Biotechnol. 85:1095-1104(2010) [PubMed: 19707751] [Abstract] Cited for: FUNCTION, PROBABLE ENZYME ACTIVITY, MUTAGENESIS OF 291-ASP-GLU-292. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U73857 Genomic DNA. Translation: AAB18109.1. U00096 Genomic DNA. Translation: AAC73488.1. AP009048 Genomic DNA. Translation: BAE76166.1. M13345 Genomic DNA. Translation: AAA83895.1.
PIR	A64767.
RefSeq	NP_414919.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0AAP1.
SMR	P0AAP1. Positions 208-370.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000002296; EBESCP00000002296; EBESCG00000001874. EBESCT00000014865; EBESCP00000014156; EBESCG00000013925.
GeneID	945037.
GenomeReviews	Gene locus JW0376 in contig AP009048_GR. Gene locus b0385 in contig U00096_GR.
KEGG	ecj:JW0376. eco:b0385.
PATRIC	32115911. VBIEscCol129921_0397.
Organism-specific databases
EchoBASE	EB1237.
EcoGene	EG11257. adrA.
Phylogenomic databases
eggNOG	COG2199.
GeneTree	EBGT00050000008781.
HOGENOM	HBG288926.
OMA	LGARHES.
PhylomeDB	P0AAP1.
ProtClustDB	PRK10245.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11257-MONOMER.
Gene expression databases
Genevestigator	P0AAP1.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. IPR000160. Diguanylate_cyclase-pred. IPR007894. MASE2. [Graphical view]
Pfam	PF00990. GGDEF. 1 hit. PF05230. MASE2. 1 hit. [Graphical view]
SMART	SM00267. GGDEF. 1 hit. [Graphical view]
SUPFAM	SSF55073. A/G_cyclase. 1 hit.
TIGRFAMs	TIGR00254. GGDEF. 1 hit.
PROSITE	PS50887. GGDEF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADRA_ECOLI

Accession

Primary (citable) accession number: P0AAP1
Secondary accession number(s): P21830, P77719, Q2MC40

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 11, 2005
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program