BIPA_ECO27
ID BIPA_ECO27 Reviewed; 607 AA.
AC P0A3B2; B7UNJ3; P32132; Q2M8G8; Q6BEY2; Q9EXN7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=50S ribosomal subunit assembly factor BipA {ECO:0000255|HAMAP-Rule:MF_00849};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:9622352};
DE AltName: Full=GTP-binding protein BipA {ECO:0000255|HAMAP-Rule:MF_00849};
DE AltName: Full=GTP-binding protein BipA/TypA;
DE AltName: Full=Ribosome-dependent GTPase BipA;
DE AltName: Full=Tyrosine phosphorylated protein A {ECO:0000303|PubMed:9642082};
GN Name=bipA {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000303|PubMed:9622352};
GN Synonyms=o591 {ECO:0000303|PubMed:9642082},
GN typA {ECO:0000303|PubMed:9642082}; OrderedLocusNames=E2348C_4177;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GTPASE ACTIVITY, CATALYTIC ACTIVITY,
RP PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=E2348/69 / EPEC / MAR001;
RX PubMed=9622352; DOI=10.1046/j.1365-2958.1998.00793.x;
RA Farris M., Grant A., Richardson T.B., O'Connor C.D.;
RT "BipA: a tyrosine-phosphorylated GTPase that mediates interactions between
RT enteropathogenic Escherichia coli (EPEC) and epithelial cells.";
RL Mol. Microbiol. 28:265-279(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7,
RP PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=E2348/69 / EPEC / MAR001;
RX PubMed=9642082; DOI=10.1006/jmbi.1998.1836;
RA Freestone P., Trinei M., Clarke S.C., Nystroem T., Norris V.;
RT "Tyrosine phosphorylation in Escherichia coli.";
RL J. Mol. Biol. 279:1045-1051(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
RN [4]
RP PROTEIN SEQUENCE OF 1-14, SUBUNIT, AND PHOSPHORYLATION.
RC STRAIN=E2348/69 / EPEC / MAR001;
RX PubMed=7783627; DOI=10.1111/j.1365-2958.1995.tb02270.x;
RA Freestone P., Grant S., Toth I., Norris V.;
RT "Identification of phosphoproteins in Escherichia coli.";
RL Mol. Microbiol. 15:573-580(1995).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=E2348/69 / EPEC / MAR001;
RX PubMed=9765944; DOI=10.1042/bst026s225;
RA Farris M., Grant A., Jane S., Chad J., O'Connor C.D.;
RT "BipA affects Ca++ fluxes and phosphorylation of the translocated intimin
RT receptor (Tir/Hp90) in host epithelial cells infected with enteropathogenic
RT E. coli.";
RL Biochem. Soc. Trans. 26:S225-S225(1998).
CC -!- FUNCTION: A 50S ribosomal subunit assembly protein with GTPase
CC activity, required for 50S subunit assembly at low temperatures, may
CC also play a role in translation. Binds GTP and analogs. Binds the 70S
CC ribosome between the 30S and 50S subunits, in a similar position as
CC ribosome-bound EF-G; it contacts a number of ribosomal proteins, both
CC rRNAs and the A-site tRNA (By similarity). GTPase that impacts
CC interactions between enteropathogenic E.coli (EPEC) and epithelial
CC cells and also has an effect on motility (PubMed:9622352).
CC {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:9622352}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00849, ECO:0000269|PubMed:9622352};
CC -!- SUBUNIT: Purifies as a 125-130 kDa band, also copurifies with RNA
CC polymerase. {ECO:0000269|PubMed:7783627}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849}.
CC Note=Binds to ribosomes. {ECO:0000255|HAMAP-Rule:MF_00849}.
CC -!- PTM: Phosphorylated on tyrosine, probably by autophosphorylation
CC (PubMed:9622352, PubMed:9642082) (Probable). Phosphorylation is
CC strongly activated by proteins present in strain E2348/69 / EPEC /
CC MAR001 but not K12 / DH5 alpha. Phosphorylation increases GTPase
CC activity (PubMed:9622352). {ECO:0000269|PubMed:9622352,
CC ECO:0000269|PubMed:9642082, ECO:0000305|PubMed:7783627}.
CC -!- DISRUPTION PHENOTYPE: Deletion alters the pattern of protein synthesis
CC during both exponential growth and carbon starvation (PubMed:9642082).
CC No longer alters host cytoskeleton; upon infection of HeLa cells
CC microvilli are not disrupted (although some thicken), bacteria adhere
CC to host cells but actin does not accumulate beneath them. 100-fold
CC increased sensitivity of bacteria to human BPI. Increased bacterial
CC cell motililty, increased secretion of flagellin gene (fliC)
CC (PubMed:9622352). Decreased accumulation in infected HeLa cells of a
CC phosphotyrosine protein that might be bacterial Tir, enhanced Ca(2+)
CC efflux from infected HeLa cells (PubMed:9765944).
CC {ECO:0000269|PubMed:9622352, ECO:0000269|PubMed:9642082,
CC ECO:0000269|PubMed:9765944}.
CC -!- MISCELLANEOUS: The initial events following infection of human cells by
CC EPEC bacteria include the destruction of microvilli and the
CC accumulation of actin underneath the adherent bacteria (part of the
CC attaching and effacing lesion). {ECO:0000303|PubMed:9622352}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. BipA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00849}.
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DR EMBL; AJ224871; CAA12172.1; -; Genomic_DNA.
DR EMBL; AJ278218; CAC20136.1; -; Genomic_DNA.
DR EMBL; FM180568; CAS11725.1; -; Genomic_DNA.
DR EMBL; AF058333; AAC13722.1; -; Genomic_DNA.
DR RefSeq; WP_000570668.1; NC_011601.1.
DR AlphaFoldDB; P0A3B2; -.
DR SMR; P0A3B2; -.
DR IntAct; P0A3B2; 50.
DR EnsemblBacteria; CAS11725; CAS11725; E2348C_4177.
DR GeneID; 66672223; -.
DR KEGG; ecg:E2348C_4177; -.
DR HOGENOM; CLU_017016_4_0_6; -.
DR OMA; MSMLFTI; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR CDD; cd03710; BipA_TypA_C; 1.
DR Gene3D; 2.40.50.250; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00849; BipA; 1.
DR InterPro; IPR035651; BipA_V.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR042116; TypA/BipA_C.
DR InterPro; IPR006298; TypA_GTP-bd.
DR PANTHER; PTHR42908:SF8; PTHR42908:SF8; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR TIGRFAMs; TIGR01394; TypA_BipA; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; GTP-binding; Hydrolase;
KW Nucleotide-binding; Phosphoprotein; Ribosome biogenesis; RNA-binding;
KW rRNA-binding; tRNA-binding; Virulence.
FT CHAIN 1..607
FT /note="50S ribosomal subunit assembly factor BipA"
FT /id="PRO_0000091551"
FT DOMAIN 3..198
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 15..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT VARIANT 489
FT /note="I -> T (in strain: MAR001)"
FT VARIANT 497
FT /note="V -> A (in strain: MAR001)"
FT CONFLICT 151
FT /note="L -> F (in Ref. 2; AAC13722)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="E -> Q (in Ref. 2; AAC13722)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="D -> H (in Ref. 2; AAC13722)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="E -> K (in Ref. 2; AAC13722)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="T -> I (in Ref. 2; AAC13722)"
FT /evidence="ECO:0000305"
FT CONFLICT 589..607
FT /note="Missing (in Ref. 2; AAC13722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 67355 MW; 3B4DE3A514F95FFB CRC64;
MIEKLRNIAI IAHVDHGKTT LVDKLLQQSG TFDSRAETQE RVMDSNDLEK ERGITILAKN
TAIKWNDYRI NIVDTPGHAD FGGEVERVMS MVDSVLLVVD AFDGPMPQTR FVTKKAFAYG
LKPIVVINKV DRPGARPDWV VDQVFDLFVN LDATDEQLDF PIVYASALNG IAGLDHEDMA
EDMTPLYQAI VDHVPAPDVD LDGPFQMQIS QLDYNSYVGV IGIGRIKRGK VKPNQQVTII
DSEGKTRNAK VGKVLGHLGL ERIETDLAEA GDIVAITGLG ELNISDTVCD TQNVEALPAL
SVDEPTVSMF FCVNTSPFCG KEGKFVTSRQ ILDRLNKELV HNVALRVEET EDADAFRVSG
RGELHLSVLI ENMRREGFEL AVSRPKVIFR EIDGRKQEPY ENVTLDVEEQ HQGSVMQALG
ERKGDLKNMN PDGKGRVRLD YVIPSRGLIG FRSEFMTMTS GTGLLYSTFS HYDDVRPGEV
GQRQNGVLIS NGQGKAVAFA LFGLQDRGKL FLGHGAEVYE GQIIGIHSRS NDLTVNCLTG
KKLTNMRASG TDEAVVLVPP IRMTLEQALE FIDDDELVEV TPTSIRIRKR HLTENDRRRA
NRAPKDD
