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Database: UniProt
Entry: A0A329MM10_9BACL
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ID   A0A329MM10_9BACL        Unreviewed;       612 AA.
AC   A0A329MM10;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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:RAV19763.1};
GN   Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN   ORFNames=DQG23_17615 {ECO:0000313|EMBL:RAV19763.1};
OS   Paenibacillus contaminans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=450362 {ECO:0000313|EMBL:RAV19763.1, ECO:0000313|Proteomes:UP000250369};
RN   [1] {ECO:0000313|EMBL:RAV19763.1, ECO:0000313|Proteomes:UP000250369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CKOBP-6 {ECO:0000313|EMBL:RAV19763.1,
RC   ECO:0000313|Proteomes:UP000250369};
RX   PubMed=19126735; DOI=10.1099/ijs.0.001495-0;
RA   Chou J.H., Lee J.H., Lin M.C., Chang P.S., Arun A.B., Young C.C.,
RA   Chen W.M.;
RT   "Paenibacillus contaminans sp. nov., isolated from a contaminated
RT   laboratory plate.";
RL   Int. J. Syst. Evol. Microbiol. 59:125-129(2009).
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:RAV19763.1}.
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DR   EMBL; QMFB01000010; RAV19763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A329MM10; -.
DR   OrthoDB; 9801591at2; -.
DR   Proteomes; UP000250369; 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:UP000250369};
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;  68449 MW;  1A4552C00DCAB3A1 CRC64;
     MHSREKIRNI AIIAHVDHGK TTLVDQLLQQ SGVFREHEAV QERAMDSGDI ERERGITILA
     KNTAIHYKDY LVNIVDTPGH ADFGGEVERI MKMVDGVVLV VDAFEGCMPQ TKFVLRKALE
     QELKPIVVVN KIDRPNARPA EVVDEVLDLF IELGANDEQL EFNVVYASGL QGTSSLDPEK
     QDSNMVALYE TIVQQIPAPT ESVDEPLQFL VTLMDYNEYL GRIGIGRVNR GIIRQGQPVA
     VMTREGAIKQ ARIEKLFGFQ GLKRVEVEQA GAGDIIAIAG IKEINIGETI ADPNKPEALP
     VLKIDEPTLQ MTFLVNNSPF AGKEGKWVTS RKLRERLFKE VETDVSLRVD ETDSPDAFIV
     SGRGELHLGI LIENMRREGF ELQVSKPEVI VKEIDGQKME PYERLIIDVP EESMGSVMES
     LGTRKAEMVN MINNSGQVRL EFLIPARGLI GYRTYFLTLT RGYGVLNHAF DSYGPYSGNN
     VGGRHQGVLV SSDTGVSTLY GILSIEDRGL LFLEPGANVY EGMIVGEHTR DNDIIVNICK
     EKQLTNIRSA GKDDTVKMKT PRIYSLEAAL EYLNDDEYCE ITPKSIRLRK KILNKSERER
     AEKHRKMAEA NA
//
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