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Database: UniProt
Entry: A0A0A1YN17_9PSED
LinkDB: A0A0A1YN17_9PSED
Original site: A0A0A1YN17_9PSED 
ID   A0A0A1YN17_9PSED        Unreviewed;       605 AA.
AC   A0A0A1YN17;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=bipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN   ORFNames=TMS3_0105120 {ECO:0000313|EMBL:KFX71307.1};
OS   Pseudomonas taeanensis MS-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX71307.1, ECO:0000313|Proteomes:UP000030063};
RN   [1] {ECO:0000313|EMBL:KFX71307.1, ECO:0000313|Proteomes:UP000030063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-3 {ECO:0000313|EMBL:KFX71307.1,
RC   ECO:0000313|Proteomes:UP000030063};
RX   PubMed=24407626;
RA   Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA   Choi J.S., Kahng H.Y., Kim S.I.;
RT   "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT   Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT   Seashore.";
RL   Genome Announc. 2:0-0(2014).
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:KFX71307.1}.
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DR   EMBL; AWSQ01000001; KFX71307.1; -; Genomic_DNA.
DR   RefSeq; WP_025164148.1; NZ_AWSQ01000001.1.
DR   AlphaFoldDB; A0A0A1YN17; -.
DR   STRING; 1395571.TMS3_0105120; -.
DR   eggNOG; COG1217; Bacteria.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000030063; 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:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
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:UP000030063};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00849};
KW   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   605 AA;  66724 MW;  A6E83EDC2AE56B90 CRC64;
     MIEKLRNIAI IAHVDHGKTT LVDALLRQSG TLERNELDTE RLMDSNDQEK ERGITILAKN
     TAINWNGHHI NIVDTPGHAD FGGEVERVMS MVDSVLLVVD AQDGPMPQTR FVTKKAFEAG
     LRPIVVVNKV DRPGARPDWV VEQIFDLFDN LGATEEQLDF PIVFASAING VAGLEHTAMA
     EDLVPLYQAI VDHVPAPQVD RDGPFQMQIS ALDYNSFLGI IGVGRIARGR VKPNTQVVAI
     DVHGKRRNGR ILKLMGHHGL HRVDVDEAAA GDIVCISGFD QLFISDTLCD PQNVEAMTPL
     SVDEPTVAMT FQVNDSPFCG KEGKFVTSRN IKERLDKELL YNVALRVEEG DSADKFKVSG
     RGELHLSVLI ETMRREGFEM GVGRPEVIIK LVDGVKHEPY ENVTIDVPEV SQGALMEQMG
     NRKGDLTNMV PDGKGRVRLE YNIPARGLIG FRNEFLTLTS GAGIMTSIFD RYDVMKSGDM
     SGRQNGVLVS VATGKALTYS LETLQARGKL FVEHGQDIYE GQIVGLNSRD NDLGVNPTKG
     KKLDNMRASG KDETIALVPP VRFTLEQALE FIQDDELCEV TPKSIRLRKK ILGESERTRA
     AKKGS
//
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