BIPA_BACSU
ID BIPA_BACSU Reviewed; 612 AA.
AC O07631;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=50S ribosomal subunit assembly factor BipA {ECO:0000255|HAMAP-Rule:MF_00849};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_00849};
DE AltName: Full=GTP-binding protein BipA {ECO:0000255|HAMAP-Rule:MF_00849};
GN Name=bipA {ECO:0000255|HAMAP-Rule:MF_00849};
GN Synonyms=ylaG {ECO:0000303|PubMed:9384377}; OrderedLocusNames=BSU14770;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Purnelle B., Presecan E., Glaser P., Richou A., Danchin A., Goffeau A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION BY COLD SHOCK, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=12399512; DOI=10.1128/jb.184.22.6395-6402.2002;
RA Beckering C.L., Steil L., Weber M.H.W., Voelker U., Marahiel M.A.;
RT "Genomewide transcriptional analysis of the cold shock response in Bacillus
RT subtilis.";
RL J. Bacteriol. 184:6395-6402(2002).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00849};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849}.
CC Note=Binds to ribosomes. {ECO:0000255|HAMAP-Rule:MF_00849}.
CC -!- INDUCTION: 3-fold induction by growth at 15 degrees Celsius.
CC {ECO:0000269|PubMed:12399512}.
CC -!- DISRUPTION PHENOTYPE: No visible growth phenotype at 15 degrees
CC Celsius. {ECO:0000269|PubMed:12399512}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. BipA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00849}.
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DR EMBL; Z97025; CAB09712.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13350.1; -; Genomic_DNA.
DR PIR; E69872; E69872.
DR RefSeq; NP_389360.1; NC_000964.3.
DR RefSeq; WP_003232278.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07631; -.
DR SMR; O07631; -.
DR IntAct; O07631; 1.
DR MINT; O07631; -.
DR STRING; 224308.BSU14770; -.
DR jPOST; O07631; -.
DR PaxDb; O07631; -.
DR PRIDE; O07631; -.
DR EnsemblBacteria; CAB13350; CAB13350; BSU_14770.
DR GeneID; 935966; -.
DR KEGG; bsu:BSU14770; -.
DR PATRIC; fig|224308.179.peg.1611; -.
DR eggNOG; COG1217; Bacteria.
DR InParanoid; O07631; -.
DR OMA; MSMLFTI; -.
DR PhylomeDB; O07631; -.
DR BioCyc; BSUB:BSU14770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
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; cd03710; BipA_TypA_C; 1.
DR Gene3D; 2.40.50.250; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00849; BipA; 1.
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 InterPro; IPR006298; TypA_GTP-bd.
DR PANTHER; PTHR42908:SF8; PTHR42908:SF8; 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR TIGRFAMs; TIGR01394; TypA_BipA; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..612
FT /note="50S ribosomal subunit assembly factor BipA"
FT /id="PRO_0000091546"
FT DOMAIN 5..200
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 17..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
SQ SEQUENCE 612 AA; 68389 MW; 87CC7921948DD7F3 CRC64;
MKLRNDLRNI AIIAHVDHGK TTLVDQLLHQ AGTFRANEQV AERAMDSNDL ERERGITILA
KNTAINYKDT RINILDTPGH ADFGGEVERI MKMVDGVVLV VDAYEGCMPQ TRFVLKKALE
QNLNPVVVVN KIDRDFARPE EVIDEVLDLF IELDANEEQL EFPVVYASAI NGTASLDPKQ
QDENMEALYE TIIKHVPAPV DNAEEPLQFQ VALLDYNDYV GRIGIGRVFR GTMKVGQQVS
LMKLDGTAKS FRVTKIFGFQ GLKRVEIEEA KAGDLVAVSG MEDINVGETV CPVDHQDPLP
VLRIDEPTLQ MTFVVNNSPF AGREGKYVTA RKIEERLQSQ LQTDVSLRVE PTASPDAWVV
SGRGELHLSI LIENMRREGY ELQVSKPEVI IKEIDGVRCE PVERVQIDVP EEHTGSVMES
MGARKGEMVD MINNGNGQVR LIFTVPSRGL IGYSTEFLSL TRGFGILNHT FDSYQPMQAG
QVGGRRQGVL VSMENGKATS YGIQGIEDRG VIFVEPGTEV YEGMIVGEHN RDNDLVVNVS
KMKQQTNVRS ATKDQTTTIK KARIMSLEES LEYLNEDEYC EVTPESIRLR KKILNKNERE
KAAKKKKTAG LS
