ID K6C338_9BACI Unreviewed; 612 AA.
AC K6C338;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=BABA_19646 {ECO:0000313|EMBL:EKN65535.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65535.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN65535.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:EKN65535.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJLS01000131; EKN65535.1; -; Genomic_DNA.
DR RefSeq; WP_007086922.1; NZ_AJLS01000131.1.
DR AlphaFoldDB; K6C338; -.
DR STRING; 1117379.BABA_19646; -.
DR PATRIC; fig|1117379.3.peg.4072; -.
DR eggNOG; COG1217; Bacteria.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000006316; 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; IPR041095; EFG_II.
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; PF14492; EFG_III; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006316};
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 5..200
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 612 AA; 68742 MW; D5E753A732D9218A CRC64;
MKLREDVRNI AIIAHVDHGK TTLVDQLLKQ SGTFRSNEHV EERAMDSGDI ERERGITILA
KNTAIQYKDT RINILDTPGH ADFGGEVERI MKMVDGVLLV VDAYEGCMPQ TRFVLKKALE
QKITPIVVVN KIDRDFARPA EVVDEVIDLF IELDATEDQL EFPVIYASGI NGTASKDPEK
QDENMQSLYD AIVEYIPAPV DNHEEPLQFQ VALLDYNDYV GRIGIGRVFR GTMHVGQQVA
LMKLDGSVKQ FRVTKIFGFF GLKREEVQEA KAGDLIAVSG MEDINVGETV CPTEHQEALP
ILRIDEPTLQ MTFAVNNSPF AGREGKYLTS RKIEERLLAQ LHTDVSLRVE NTDSPDAWIV
SGRGELHLSI LIENMRREGY ELQVSKPEVI VKVIDGVRCE PVERVQIDVP EEHTGSVMES
IGARKGEMLD MINNGSGQVR LIFNVPARGL IGYTTEFLTM TRGYGIINHT FDSYQPMLSG
QVGGRHQGVL VSMESGKAST YGIMQVEDRG TIFVEPGTEI YEGMIVGENT RENDITVNIT
KVKQATNVRS ANKDQTSVIK KPRIMTLEES LEYLNDDEYC EVTPESIRLR KKILDKNERE
KSAKKKKYAE MS
//
