BIPA_SHIFL
ID BIPA_SHIFL Reviewed; 607 AA.
AC P0A3B4; Q9EXN7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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};
DE AltName: Full=GTP-binding protein BipA {ECO:0000255|HAMAP-Rule:MF_00849};
GN Name=bipA {ECO:0000255|HAMAP-Rule:MF_00849};
GN OrderedLocusNames=SF3941, S3805;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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. {ECO:0000255|HAMAP-Rule:MF_00849}.
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};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849}.
CC Note=Binds to ribosomes. {ECO:0000255|HAMAP-Rule:MF_00849}.
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; AE005674; AAN45376.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18822.1; -; Genomic_DNA.
DR RefSeq; NP_709669.1; NC_004337.2.
DR RefSeq; WP_000570668.1; NZ_UIQL01000063.1.
DR AlphaFoldDB; P0A3B4; -.
DR SMR; P0A3B4; -.
DR STRING; 198214.SF3941; -.
DR PRIDE; P0A3B4; -.
DR DNASU; 1080929; -.
DR EnsemblBacteria; AAN45376; AAN45376; SF3941.
DR EnsemblBacteria; AAP18822; AAP18822; S3805.
DR GeneID; 1025901; -.
DR GeneID; 66672223; -.
DR KEGG; sfl:SF3941; -.
DR KEGG; sfx:S3805; -.
DR PATRIC; fig|198214.7.peg.4645; -.
DR HOGENOM; CLU_017016_4_0_6; -.
DR OrthoDB; 143460at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..607
FT /note="50S ribosomal subunit assembly factor BipA"
FT /id="PRO_0000091557"
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 CONFLICT 319
FT /note="C -> S (in Ref. 2; AAP18822)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="E -> K (in Ref. 2; AAP18822)"
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
