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Database: UniProt
Entry: I8AGW6_9BACI
LinkDB: I8AGW6_9BACI
Original site: I8AGW6_9BACI 
ID   I8AGW6_9BACI            Unreviewed;       612 AA.
AC   I8AGW6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=A374_12860 {ECO:0000313|EMBL:EIT84937.1};
OS   Fictibacillus macauensis ZFHKF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT84937.1, ECO:0000313|Proteomes:UP000004080};
RN   [1] {ECO:0000313|EMBL:EIT84937.1, ECO:0000313|Proteomes:UP000004080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT84937.1,
RC   ECO:0000313|Proteomes:UP000004080};
RX   PubMed=22887677; DOI=10.1128/JB.01049-12;
RA   Cai L., Zhang T.;
RT   "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL   J. Bacteriol. 194:4780-4780(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:EIT84937.1}.
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DR   EMBL; AKKV01000028; EIT84937.1; -; Genomic_DNA.
DR   RefSeq; WP_007202650.1; NZ_AKKV01000028.1.
DR   AlphaFoldDB; I8AGW6; -.
DR   STRING; 1196324.A374_12860; -.
DR   PATRIC; fig|1196324.3.peg.2631; -.
DR   eggNOG; COG1217; Bacteria.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000004080; 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: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; 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:UP000004080};
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;  68951 MW;  EEEC938E2B3BD675 CRC64;
     MKFRQDIKNI AIIAHVDHGK TTLVDQMLHQ SGTFRSNEQV NERAMDSNDL EKERGITILA
     KNTAINYEGT RINIMDTPGH ADFGGEVERI MRMVDGVLLV VDAYEGCMPQ TRFVLKKALE
     QKLTPIVVVN KIDRDFARPE EVVDEVIDLF IELGADEEQL EFPVVYASAL KGTASNDPNQ
     QDEDMTALFD SIIENIPSPV DNSDESLQFQ VSLLDYNDYL GRIGIGRVFR GTMTVGQAVT
     LMKLDGTMKK FRVTKIFGFL GLKRVEIQEA KAGDLVAVSG MEEINVGETV CPEGQEEALP
     VLRIDEPTLK MTFLVNNSPF AGREGKWVTS RKIEERLRAQ LETDVSLRVD NTESPDAWVV
     SGRGELHLSI LIENMRREGY ELQVSKPEVI VRMIDGVRSE PVEHVQIDIP EEYTGAVMES
     LGERKGEMKN MVNNGSGQVR LEFMVPARGL IGYSTEFLTQ TRGYGILNHT FDSYQPMHDG
     QVGGRRQGVL VSMENGKASQ YGILNVEDRG TIFVEPGTEV YEGMIVGEHT RENDITVNIT
     KVKQMTNMRS ANKDQTVSMK KPRVMSLEEA LEYLNEDEYC EVTPESIRLR KKILDKNERE
     RQSKKKKIAT QN
//
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