Flagellar motor switch protein FliG - Helicobacter pylori (strain ATCC 700392 / 26695)

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O25119 (FLIG_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Flagellar motor switch protein FliG

Alternative name(s):
Flagellar motor switch protein G

Gene names

Name:	fliG
Ordered Locus Names:	C694_01785, HP_0352

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY. Ref.3 Ref.4
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Bacterial flagellum basal body By similarity.
Disruption phenotype	Nonflagellate. Forms dense colonies without swarming in contrast to the wild-type which forms diffuse colonies with large, swarming halos. Expression of flagellins FlaA and FlaB and the hook protein FlgE greatly reduced. Ref.3
Sequence similarities	Belongs to the FliG family.

Ontologies

Keywords
Biological process	Chemotaxis Flagellar rotation
Cellular component	Bacterial flagellum Cell inner membrane Cell membrane Membrane
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bacterial-type flagellar swarming motility Inferred from mutant phenotype Ref.3. Source: UniProtKB chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	bacterial-type flagellum Inferred from mutant phenotype Ref.3. Source: UniProtKB bacterial-type flagellum basal body Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	motor 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 – 343

343

Flagellar motor switch protein FliG

PRO_0000421839

Regions

Motif

137 – 140

Part of the EHPQR-motif

Motif

245 – 248

M-F-X-F motif; its intrinsic flexibility is probably coupled to flagellar rotation

Sites

Site

172

Part of the EHPQR-motif

Experimental info

Mutagenesis

209

R → C: A prominent downward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4

Mutagenesis

217

R → C: A slight downward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4

Mutagenesis

222

S → C: A prominent downward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4

Mutagenesis

243

E → C: A complete upward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4

Mutagenesis

325

Q → C: No mobility shift in SDS-PAGE nor reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking. A mobility shift and reduction in the fluorescence intensity after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated either with C-209; C-217; C-222 or C-243. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

O25119 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 861214ED1782980A
Show »

FASTA

343

38,326

        10         20         30         40         50         60 
MATKLTPKQK AQLDELSMSE KIAILLIQVG EDTTGEILRH LDIDSITEIS KQIVQLNGTD 

        70         80         90        100        110        120 
KQIGAAVLEE FFAIFQSNQY INTGGLEYAR ELLTRTLGSE EAKKVMDKLT KSLQTQKNFA 

       130        140        150        160        170        180 
YLGKIKPQQL ADFIINEHPQ TIALILAHME APNAAETLSY FPDEMKAEIS IRMANLGEIS 

       190        200        210        220        230        240 
PQVVKRVSTV LENKLESLTS YKIEVGGLRA VAEIFNRLGQ KSAKTTLARI ESVDNKLAGA 

       250        260        270        280        290        300 
IKEMMFTFED IVKLDNFAIR EILKVADKKD LSLALKTSTK DLTDKFLNNM SSRAAEQFVE 

       310        320        330        340 
EMQYLGAVKI KDVDVAQRKI IEIVQSLQEK GVIQTGEEED VIE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C. Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.
[2]	"Draft genome of Helicobacter pylori." Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D., Kostrjukova E., Govorun V. Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.
[3]	"Mutational analysis of genes encoding the early flagellar components of Helicobacter pylori: evidence for transcriptional regulation of flagellin A biosynthesis." Allan E., Dorrell N., Foynes S., Anyim M., Wren B.W. J. Bacteriol. 182:5274-5277(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: SS1.
[4]	"Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching." Lam K.H., Ip W.S., Lam Y.W., Chan S.O., Ling T.K., Au S.W. Structure 20:315-325(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 86-343, FUNCTION, MOTIF, MUTAGENESIS OF ARG-209; ARG-217; SER-222; GLU-243 AND GLN-325. Strain: ATCC 700392 / 26695.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000511 Genomic DNA. Translation: AAD07420.1.
CP003904 Genomic DNA. Translation: AFV41574.1.

PIR

H64563.

RefSeq

NP_207150.1. NC_000915.1.
YP_006934277.1. NC_018939.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3USW	X-ray	2.60	A	86-343	[»]
3USY	X-ray	2.71	A/B	116-343	[»]

ProteinModelPortal

O25119.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3534N.

MINT

MINT-166826.

STRING

85962.HP0352.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD07420; AAD07420; HP_0352.

GeneID

13869536.
899214.

KEGG

heo:C694_01785.
hpy:HP0352.

PATRIC

20591937. VBIHelPyl33062_0365.

Phylogenomic databases

K02410.

OMA

FIQDEHP.

ProtClustDB

PRK05686.

Family and domain databases

InterPro

IPR000090. Flg_Motor_Flig.
IPR011002. FliG_a-hlx.
[Graphical view]

PIRSF

PIRSF003161. FliG. 1 hit.

PRINTS

PR00954. FLGMOTORFLIG.

SUPFAM

SSF48029. FliG_like. 2 hits.

TIGRFAMs

TIGR00207. fliG. 1 hit.

ProtoNet

Search...

Entry information

Entry name

FLIG_HELPY

Accession

Primary (citable) accession number: O25119

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2013
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents