ID C4ZPS7_THASP Unreviewed; 605 AA.
AC C4ZPS7; A0A5C7STF2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
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 Synonyms=typA {ECO:0000313|EMBL:TXH86843.1};
GN OrderedLocusNames=Tmz1t_2183 {ECO:0000313|EMBL:ACK54923.1};
GN ORFNames=E6Q80_06950 {ECO:0000313|EMBL:TXH86843.1};
OS Thauera aminoaromatica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=164330 {ECO:0000313|EMBL:ACK54923.1, ECO:0000313|Proteomes:UP000002186};
RN [1] {ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACK54923.1, ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|EMBL:ACK54923.1,
RC ECO:0000313|Proteomes:UP000002186};
RX PubMed=23407619; DOI=10.4056/sigs.2696029;
RA Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL Stand. Genomic Sci. 6:325-335(2012).
RN [3] {ECO:0000313|EMBL:TXH86843.1, ECO:0000313|Proteomes:UP000321192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin_27_1 {ECO:0000313|EMBL:TXH86843.1};
RA Stamps B.W., Spear J.R.;
RT "Metagenome Assembled Genomes from an Advanced Water Purification
RT Facility.";
RL Submitted (SEP-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}.
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DR EMBL; CP001281; ACK54923.1; -; Genomic_DNA.
DR EMBL; SSFD01000098; TXH86843.1; -; Genomic_DNA.
DR RefSeq; WP_004301400.1; NZ_SSFD01000098.1.
DR AlphaFoldDB; C4ZPS7; -.
DR STRING; 85643.Tmz1t_2183; -.
DR KEGG; tmz:Tmz1t_2183; -.
DR eggNOG; COG1217; Bacteria.
DR HOGENOM; CLU_017016_4_0_4; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000002186; Chromosome.
DR Proteomes; UP000321192; 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 SMART; SM00838; EFG_C; 1.
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|HAMAP-Rule:MF_00849};
KW Reference proteome {ECO:0000313|Proteomes:UP000002186};
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; 67251 MW; C6D6EFD16D56DA98 CRC64;
MSRAIRNIAI IAHVDHGKTT LVDQLLRQSG TFRENQQVAE RVMDSGDIEK ERGITILSKN
CAIQYGDTHI NIVDTPGHAD FGGEVERVLS MVDSVLLLVD AVEGPMPQTR FVTRKALALG
LKPIVVINKI DRPGARPDWV INHTFDLFDK LGATEEQLDF PVIYASGLNG FAVINEGDER
KDMRPLFEAI LEHVPAPEVD ANGPLQIQVC SLDYSTYMGQ LGIGRIKRGS VRPNQEVVVM
YGEENRGKGK VSQILTFEGL ERKPSELAEA GDIVLIAGIQ QVNIGVTLCD PECLEGMKPI
AVDEPTLTMN FMVNTSPLAG REGKYVTSRQ IRERLEKELL KNVALRVNYT GDSDVFEVSG
RGELHLTILL ENMRREGYEL AVGRPRVVYK EIDGVKCEPY EMLTVDVEED HQGSVMEELG
RRRGELQDMQ PDGRGRVRLE YRIPARGLIG FQGEFLTMTR GTGLASHVFD DYGPMAGAMA
ERRNGVLISQ NDGDAVAYAL WNLQDRGRMF VSPGEALYEG MIIGIHTRDN DLVVNPIKGK
QLTNVRASGT DEAVRLITPI QLTLESAIEF IADDELVEIT PKNIRLRKRH LKETDRKRAA
KADAS
//
