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Protein

GTP-binding protein TypA/BipA

Gene

typA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably interacts with the ribosomes in a GTP dependent manner. GTPase that mediates interactions between enteropathogenic E.coli (EPEC) and epithelial cells.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi74 – 785GTPBy similarity
Nucleotide bindingi128 – 1314GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • response to cold Source: EcoCyc
  • response to heat Source: EcoCyc
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11837-MONOMER.
ECOL316407:JW5571-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein TypA/BipA
Alternative name(s):
Tyrosine phosphorylated protein A
Gene namesi
Name:typA
Synonyms:bipA, yihK
Ordered Locus Names:b3871, JW5571
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11837. typA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607GTP-binding protein TypA/BipAPRO_0000091550Add
BLAST

Post-translational modificationi

Phosphorylated on tyrosine residues.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP32132.
PaxDbiP32132.
PRIDEiP32132.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
rlmLP758643EBI-562154,EBI-547718

Protein-protein interaction databases

BioGridi4262631. 10 interactions.
DIPiDIP-11058N.
IntActiP32132. 5 interactions.
STRINGi511145.b3871.

Structurei

Secondary structure

1
607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Helixi18 – 2710Combined sources
Beta strandi59 – 657Combined sources
Beta strandi68 – 747Combined sources
Beta strandi81 – 833Combined sources
Helixi84 – 896Combined sources
Beta strandi93 – 1008Combined sources
Turni101 – 1033Combined sources
Helixi107 – 1093Combined sources
Helixi110 – 1189Combined sources
Beta strandi123 – 1286Combined sources
Helixi137 – 14711Combined sources
Turni148 – 1514Combined sources
Helixi154 – 1574Combined sources
Beta strandi162 – 1665Combined sources
Turni167 – 1704Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi181 – 1833Combined sources
Helixi184 – 19310Combined sources
Beta strandi200 – 2034Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi211 – 2155Combined sources
Turni216 – 2183Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi228 – 2314Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi278 – 2814Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi307 – 3126Combined sources
Turni317 – 3204Combined sources
Helixi328 – 33811Combined sources
Turni339 – 3413Combined sources
Beta strandi346 – 3494Combined sources
Beta strandi355 – 3628Combined sources
Helixi363 – 37513Combined sources
Beta strandi380 – 3823Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi395 – 40814Combined sources
Helixi409 – 42113Combined sources
Beta strandi425 – 4317Combined sources
Beta strandi435 – 44410Combined sources
Helixi445 – 4484Combined sources
Helixi451 – 4599Combined sources
Beta strandi464 – 47411Combined sources
Beta strandi485 – 4906Combined sources
Helixi498 – 5047Combined sources
Helixi505 – 5073Combined sources
Beta strandi508 – 5114Combined sources
Beta strandi522 – 53110Combined sources
Beta strandi533 – 5353Combined sources
Helixi542 – 5465Combined sources
Helixi565 – 5717Combined sources
Beta strandi576 – 5816Combined sources
Beta strandi584 – 5918Combined sources
Helixi594 – 6018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZCIX-ray2.63A/B1-601[»]
4ZCKX-ray2.48A306-603[»]
4ZCLX-ray3.06A/B1-601[»]
4ZCMX-ray3.31A/B1-607[»]
5A9WX-ray3.70A1-607[»]
5A9XX-ray3.80A1-607[»]
5A9YX-ray4.00A1-607[»]
ProteinModelPortaliP32132.
SMRiP32132. Positions 1-604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 198196tr-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. TypA subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CI3. Bacteria.
COG1217. LUCA.
HOGENOMiHOG000282351.
InParanoidiP32132.
KOiK06207.
OMAiSMLFTIN.
OrthoDBiEOG67HJSM.
PhylomeDBiP32132.

Family and domain databases

Gene3Di3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR006298. TypA_GTP-bd.
[Graphical view]
PANTHERiPTHR23115:SF14. PTHR23115:SF14. 1 hit.
PfamiPF00679. EFG_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
TIGR01394. TypA_BipA. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEKLRNIAI IAHVDHGKTT LVDKLLQQSG TFDSRAETQE RVMDSNDLEK
60 70 80 90 100
ERGITILAKN TAIKWNDYRI NIVDTPGHAD FGGEVERVMS MVDSVLLVVD
110 120 130 140 150
AFDGPMPQTR FVTKKAFAYG LKPIVVINKV DRPGARPDWV VDQVFDLFVN
160 170 180 190 200
LDATDEQLDF PIVYASALNG IAGLDHEDMA EDMTPLYQAI VDHVPAPDVD
210 220 230 240 250
LDGPFQMQIS QLDYNSYVGV IGIGRIKRGK VKPNQQVTII DSEGKTRNAK
260 270 280 290 300
VGKVLGHLGL ERIETDLAEA GDIVAITGLG ELNISDTVCD TQNVEALPAL
310 320 330 340 350
SVDEPTVSMF FCVNTSPFCG KEGKFVTSRQ ILDRLNKELV HNVALRVEET
360 370 380 390 400
EDADAFRVSG RGELHLSVLI ENMRREGFEL AVSRPKVIFR EIDGRKQEPY
410 420 430 440 450
ENVTLDVEEQ HQGSVMQALG ERKGDLKNMN PDGKGRVRLD YVIPSRGLIG
460 470 480 490 500
FRSEFMTMTS GTGLLYSTFS HYDDVRPGEV GQRQNGVLIS NGQGKAVAFA
510 520 530 540 550
LFGLQDRGKL FLGHGAEVYE GQIIGIHSRS NDLTVNCLTG KKLTNMRASG
560 570 580 590 600
TDEAVVLVPP IRMTLEQALE FIDDDELVEV TPTSIRIRKR HLTENDRRRA

NRAPKDD
Length:607
Mass (Da):67,355
Last modified:October 11, 2004 - v2
Checksum:i3B4DE3A514F95FFB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti592 – 60716Missing (PubMed:9622352).CuratedAdd
BLAST
Sequence conflicti592 – 60716Missing (PubMed:8346018).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti489 – 4891I → T in strain: MAR001.
Natural varianti497 – 4971V → A in strain: MAR001.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224871 Genomic DNA. Translation: CAA12172.1.
L19201 Genomic DNA. Translation: AAB03005.1.
U00096 Genomic DNA. Translation: AAT48232.1.
AP009048 Genomic DNA. Translation: BAE77438.1.
PIRiS40816.
RefSeqiWP_000570668.1. NZ_LN832404.1.
YP_026274.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48232; AAT48232; b3871.
BAE77438; BAE77438; BAE77438.
GeneIDi948369.
KEGGiecj:JW5571.
eco:b3871.
PATRICi32123245. VBIEscCol129921_3983.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224871 Genomic DNA. Translation: CAA12172.1.
L19201 Genomic DNA. Translation: AAB03005.1.
U00096 Genomic DNA. Translation: AAT48232.1.
AP009048 Genomic DNA. Translation: BAE77438.1.
PIRiS40816.
RefSeqiWP_000570668.1. NZ_LN832404.1.
YP_026274.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZCIX-ray2.63A/B1-601[»]
4ZCKX-ray2.48A306-603[»]
4ZCLX-ray3.06A/B1-601[»]
4ZCMX-ray3.31A/B1-607[»]
5A9WX-ray3.70A1-607[»]
5A9XX-ray3.80A1-607[»]
5A9YX-ray4.00A1-607[»]
ProteinModelPortaliP32132.
SMRiP32132. Positions 1-604.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262631. 10 interactions.
DIPiDIP-11058N.
IntActiP32132. 5 interactions.
STRINGi511145.b3871.

Proteomic databases

EPDiP32132.
PaxDbiP32132.
PRIDEiP32132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48232; AAT48232; b3871.
BAE77438; BAE77438; BAE77438.
GeneIDi948369.
KEGGiecj:JW5571.
eco:b3871.
PATRICi32123245. VBIEscCol129921_3983.

Organism-specific databases

EchoBASEiEB1783.
EcoGeneiEG11837. typA.

Phylogenomic databases

eggNOGiENOG4105CI3. Bacteria.
COG1217. LUCA.
HOGENOMiHOG000282351.
InParanoidiP32132.
KOiK06207.
OMAiSMLFTIN.
OrthoDBiEOG67HJSM.
PhylomeDBiP32132.

Enzyme and pathway databases

BioCyciEcoCyc:EG11837-MONOMER.
ECOL316407:JW5571-MONOMER.

Miscellaneous databases

PROiP32132.

Family and domain databases

Gene3Di3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR006298. TypA_GTP-bd.
[Graphical view]
PANTHERiPTHR23115:SF14. PTHR23115:SF14. 1 hit.
PfamiPF00679. EFG_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
TIGR01394. TypA_BipA. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells."
    Farris M., Grant A., Richardson T.B., O'Connor C.D.
    Mol. Microbiol. 28:265-279(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MAR001.
  2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: SEQUENCE REVISION TO 592-607.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  7. "Identification of phosphoproteins in Escherichia coli."
    Freestone P., Grant S., Toth I., Norris V.
    Mol. Microbiol. 15:573-580(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, PROTEIN SEQUENCE OF 1-14.
  8. Cited for: PHOSPHORYLATION, PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiTYPA_ECOLI
AccessioniPrimary (citable) accession number: P32132
Secondary accession number(s): Q2M8G8, Q6BEY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 11, 2004
Last modified: July 6, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.