ID E2SQE1_9FIRM Unreviewed; 611 AA.
AC E2SQE1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:EFP60259.1};
GN Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN ORFNames=HMPREF0983_03438 {ECO:0000313|EMBL:EFP60259.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP60259.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP60259.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP60259.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) 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:EFP60259.1}.
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DR EMBL; ACTJ01000079; EFP60259.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SQE1; -.
DR STRING; 658659.HMPREF0983_03438; -.
DR eggNOG; COG1217; Bacteria.
DR HOGENOM; CLU_017016_4_0_9; -.
DR Proteomes; UP000006223; 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: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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00849}; 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 5..207
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
SQ SEQUENCE 611 AA; 68805 MW; 2A08029AA7B985FA CRC64;
MNEKEKIINI AVIAHVDAGK STLVDAFLRQ SDVFRSNEEV VDCVMDSNDL ERERGITIYS
KNCSVIHDGV KINIVDTPGH ADFSSEVERI IKTVDAVILL VDSSEGPMPQ TRFVLSKSLE
MGLRPILLIN KIDKKDARPQ EVVDEVYELF LDLNATDAQL DFPILYGIAK QGIVQYDMDT
PSDSIEPLFK TILKHCEAYP DLDEEPLQMQ ISALGYDEYI GRLGIGRIYQ GVLKAQQSVV
ICDSFGHERT NTTSQIFVYR GLSRVSVKEA RSGDIVVIAG IPDIMIGETL CEKDHIMPLE
SIHIEEPTLS MNFIVNKSPF AGKSGKYVTS RNLKERLEKE LEVNVGLKVE PTDSGDCFKV
SGRGELHISV LLEQMRREGY EVAVSKPEVI LHKDENGKTV EPVEEVVALA PEEYSGTIIN
KLNLRKGVMV DMVEENGYCR ITYEAPTRGL LGYRSEFIND TRGEGTLVRR IKGYTPYKGE
ITQRSNGAMI STETGSAMTY ALWNLQERGT LFISPQTEVY EGMIIGESAR NVDMDVNPLK
NKKLTAIRSS GNDEAMRLTP PREMSLEEAL EWINDDELVE ITPDSIRLRK KGLKPHERRQ
YYRERVQDEV K
//
