BIPA_HELPJ
ID BIPA_HELPJ Reviewed; 599 AA.
AC Q9ZLZ3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
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}; OrderedLocusNames=jhp_0432;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06013.1; -; Genomic_DNA.
DR PIR; H71932; H71932.
DR RefSeq; WP_000790195.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZLZ3; -.
DR SMR; Q9ZLZ3; -.
DR STRING; 85963.jhp_0432; -.
DR EnsemblBacteria; AAD06013; AAD06013; jhp_0432.
DR GeneID; 66521702; -.
DR KEGG; hpj:jhp_0432; -.
DR PATRIC; fig|85963.30.peg.576; -.
DR eggNOG; COG1217; Bacteria.
DR OMA; MSMLFTI; -.
DR Proteomes; UP000000804; 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; Ribosome biogenesis;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..599
FT /note="50S ribosomal subunit assembly factor BipA"
FT /id="PRO_0000091556"
FT DOMAIN 2..197
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
SQ SEQUENCE 599 AA; 66648 MW; ADD86F4D80E21BB9 CRC64;
MKNIRNIAVI AHVDHGKTTL VDGLLSQSGT FSEREKVDER VMDSNDLEKE RGITILSKNT
AIYYKDTKIN IIDTPGHADF GGEVERVLKM VDGVLLLVDA QEGVMPQTKF VVKKALSFGI
CPIVVVNKID KPAAEPDRVV DEVFDLFVAM GASDKQLDFP VVYAAARDGY AMKSLDDEKK
NLEPLFETIL EHVPSPSGSV DEPLQMQIFT LDYDNYVGKI GIARVFNGSV KKNESVLLMK
SDGSKENGRI TKLIGFLGLA RTEIENAYAG DIVALAGFNA MDVGDSVVDP TNPMPLDPMH
LEEPTMSVYF AVNDSPLAGL EGKHVTANKL KDRLLKEMQT NIAMKCEEMG EGKFKVSGRG
ELQITILAEN LRREGFEFSI SRPEVIIKEE NGVKCEPFEH LVIDTPQDFS GAIIERLGKR
KAEMKAMNPM SDGYTRLEFE IPARGLIGYR SEFLTDTKGE GVMNHSFLEF RPFSGSVESR
KNGALISMEN GEATAFSLFN IQERGALFIN PQTKVYVGMV IGEHSRDNDL DVNPIKSKHL
TNMRASGSDD AIKLTPPRTM VLERALEWIE EDEILEVTPL NLRIRKKILD PNMRKRAKK
