ID A0A1E7YYC7_9GAMM Unreviewed; 607 AA.
AC A0A1E7YYC7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Large ribosomal subunit assembly factor BipA {ECO:0000256|HAMAP-Rule:MF_00849};
DE EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_00849};
DE AltName: Full=GTP-binding protein BipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN Name=typA {ECO:0000313|EMBL:RAP71799.1};
GN Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN ORFNames=ACZ87_01381 {ECO:0000313|EMBL:RAP71799.1}, BBW68_12575
GN {ECO:0000313|EMBL:OFC61502.1};
OS Candidatus Erwinia dacicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=252393 {ECO:0000313|EMBL:OFC61502.1, ECO:0000313|Proteomes:UP000243534};
RN [1] {ECO:0000313|EMBL:OFC61502.1, ECO:0000313|Proteomes:UP000243534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL {ECO:0000313|EMBL:OFC61502.1,
RC ECO:0000313|Proteomes:UP000243534};
RA Yuval B.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAP71799.1, ECO:0000313|Proteomes:UP000244334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oroville {ECO:0000313|EMBL:RAP71799.1,
RC ECO:0000313|Proteomes:UP000244334};
RA Estes A.M., Hearn D.J., Agarwal S., Pierson E.A., Dunning-Hotopp J.C.;
RT "Genomes of the Obligate Erwinia dacicola and Facultative Enterobacter sp.
RT OLF Endosymbionts of the Olive Fruit fly, Bactrocera oleae.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00849};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00849}.
CC Note=Binds to ribosomes. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00849}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFC61502.1}.
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DR EMBL; MAYS01000385; OFC61502.1; -; Genomic_DNA.
DR EMBL; LJAM02000097; RAP71799.1; -; Genomic_DNA.
DR RefSeq; WP_070135376.1; NZ_MAYS01000385.1.
DR AlphaFoldDB; A0A1E7YYC7; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000243534; Unassembled WGS sequence.
DR Proteomes; UP000244334; Unassembled WGS sequence.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd16263; BipA_III; 1.
DR CDD; cd03710; BipA_TypA_C; 1.
DR CDD; cd03691; BipA_TypA_II; 1.
DR CDD; cd01891; TypA_BipA; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 2.40.50.250; bipa protein; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00849; BipA; 1.
DR InterPro; IPR006298; BipA.
DR InterPro; IPR048876; BipA_C.
DR InterPro; IPR047041; BipA_GTP-bd_dom.
DR InterPro; IPR047042; BipA_II.
DR InterPro; IPR047043; BipA_III.
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 NCBIfam; TIGR00231; small_GTP; 1.
DR NCBIfam; TIGR01394; TypA_BipA; 1.
DR PANTHER; PTHR42908:SF8; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF21018; BipA_C; 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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00849};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00849}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00849};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00849}; Reference proteome {ECO:0000313|Proteomes:UP000244334};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00849}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00849};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00849};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00849}.
FT DOMAIN 3..198
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 15..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
SQ SEQUENCE 607 AA; 67574 MW; 62E35323421EB912 CRC64;
MIENLRNIAI IAHVDHGKTT LVDKLLQQSG TFDPRTEATE RVMDSNDLEK ERGITILAKN
TAIKWNDYRI NIVDTPGHAD FGGEVERVMS MVDSVLLVVD AMDGPMPQTR FVTQKAFANG
LKPIVVINKV DRHGARPDWV VDQVFDLFVN LDATDEQLDF PIIYASALNG IAGLDHADMA
EDMTPLYEAI VKHVSPPQVE LETPLQMQIS QLDYNNYLGV IGIGRIKRGK VRPNQQVTII
DSEGKTRNGK VGKVLGHMGL ERIESAEAEA GDIIAITGLG ELNISDTICD MQNVQALPAL
SVDEPTVTMF FCVNTSPFCG KEGKYVTSRQ ILDRLNKELV HNVALRVEET PDADAFRVSG
RGELHLSVLI ENMRREGFEL AVSRPKVIFR EFEGRKQEPF ENVTLDIEEQ HRGSVMQAMG
ERKGDIKNMD LYGKGRVRLD YEIPSRGLIG FRNEFMTMTS GTGLLYSTFS HYDDIRPGEV
GQRQNGVLIS NGQGKAVAFA LFGLQDRGRL FLGHGAEVYE GQIIGIHSRS NDLTVNCLTG
KKLTNMRASG TDEATTLVPT QKMSLEQALE FIDDDELVEV TPQSVRIRKR HLTENDRKRA
SRGPKEA
//
