BIPA_SALTY
ID BIPA_SALTY Reviewed; 607 AA.
AC H9L427;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
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, ECO:0000269|PubMed:18621905};
DE AltName: Full=GTP-binding protein BipA {ECO:0000255|HAMAP-Rule:MF_00849};
DE AltName: Full=Ribosome-dependent GTPase BipA {ECO:0000303|PubMed:18621905};
GN Name=bipA {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000303|PubMed:8559071};
GN OrderedLocusNames=STM4009;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP INDUCTION BY BPI.
RX PubMed=8559071; DOI=10.1111/j.1365-2958.1995.mmi_17030523.x;
RA Qi S.Y., Li Y., Szyroki A., Giles I.G., Moir A., O'Connor C.D.;
RT "Salmonella typhimurium responses to a bactericidal protein from human
RT neutrophils.";
RL Mol. Microbiol. 17:523-531(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-18.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720, and SB300A;
RX PubMed=18621905; DOI=10.1128/jb.00763-08;
RA deLivron M.A., Robinson V.L.;
RT "Salmonella enterica serovar Typhimurium BipA exhibits two distinct
RT ribosome binding modes.";
RL J. Bacteriol. 190:5944-5952(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS
RP OF ARG-375; 422-ARG-LYS-423; LYS-427; 434-LYS--ARG-436; ARG-507; LYS-509;
RP HIS-527; ARG-529; ASN-536; LYS-541; LYS-542; THR-544; ARG-547; LYS-562;
RP ARG-586; ARG-588 AND 597-ARG--GLU-607.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720, and SB300A;
RX PubMed=19803466; DOI=10.1021/bi901026z;
RA deLivron M.A., Makanji H.S., Lane M.C., Robinson V.L.;
RT "A novel domain in translational GTPase BipA mediates interaction with the
RT 70S ribosome and influences GTP hydrolysis.";
RL Biochemistry 48:10533-10541(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 (By similarity). A ribosome-stimulated
CC GTPase, GTPase activity increases 4 fold in the presence of 70S
CC ribosomes. Bind to 70S ribosomes in the presence of GTP or its non-
CC hydrolyzable analog GMPPNP; in the presence of ppGpp or under stress
CC conditions it binds to 30S ribosomal subunits (PubMed:18621905,
CC PubMed:19803466). {ECO:0000255|HAMAP-Rule:MF_00849,
CC ECO:0000269|PubMed:18621905, ECO:0000269|PubMed:19803466}.
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, ECO:0000269|PubMed:18621905,
CC ECO:0000269|PubMed:19803466};
CC -!- ACTIVITY REGULATION: Ribosome-associated GTPase is not affected by low
CC levels of ppGpp, >40 uM ppGpp and >50 uM GDP inhibit GTPase
CC (PubMed:18621905). The C-terminus (residues 387-607 or 481-607)
CC inhibits GTPase activity, in its absence kcat increases, but GTPase is
CC no longer stimulated by 70S ribosome or 30S or 50S subunits
CC (PubMed:19803466). {ECO:0000269|PubMed:18621905,
CC ECO:0000269|PubMed:19803466}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00849,
CC ECO:0000269|PubMed:18621905}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849,
CC ECO:0000305|PubMed:18621905}. Note=During exponential growth the GTP-
CC bound state associates 1:1 with 70S ribosomes. Under stress conditions
CC (induction of the stringent response, growth at 42 or 16 degrees
CC Celsius) associates with 30S ribosomal subunits only.
CC {ECO:0000269|PubMed:18621905}.
CC -!- INDUCTION: Induced 7-fold when cells are treated with human
CC bactericidal permeability-increasing protein (BPI, AC P17213) (at
CC protein level). {ECO:0000269|PubMed:8559071}.
CC -!- DOMAIN: Has 5 domains; domain I (residues 1-202, also called the G
CC domain), II (203-305, also called the beta barrel domain), III (306-
CC 386) V (387-479) and the C-terminal domain (CTD 480-607) which is BipA-
CC specific. Domains I-V are homologous to domains in EF-G and LepA;
CC although the domains are similar, their relative arrangement among
CC these proteins is different. Domains I and II are not required for
CC ribosome binding, although in their absence no 30S binding under stress
CC is seen, whereas domains III, V and the CTD are required to bind both
CC 70S and 30S ribosomes. The data suggests interdomain communication
CC modulates GTPase and ribosome binding. {ECO:0000269|PubMed:19803466}.
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; AE006468; AAL22848.1; -; Genomic_DNA.
DR PIR; S70722; S70722.
DR RefSeq; NP_462889.1; NC_003197.2.
DR RefSeq; WP_000572067.1; NC_003197.2.
DR AlphaFoldDB; H9L427; -.
DR SMR; H9L427; -.
DR STRING; 99287.STM4009; -.
DR PaxDb; H9L427; -.
DR EnsemblBacteria; AAL22848; AAL22848; STM4009.
DR GeneID; 1255535; -.
DR KEGG; stm:STM4009; -.
DR PATRIC; fig|99287.12.peg.4224; -.
DR HOGENOM; CLU_017016_4_0_6; -.
DR OMA; MSMLFTI; -.
DR PhylomeDB; H9L427; -.
DR BioCyc; SENT99287:STM4009-MON; -.
DR Proteomes; UP000001014; 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; 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; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
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 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..607
FT /note="50S ribosomal subunit assembly factor BipA"
FT /id="PRO_0000449251"
FT DOMAIN 3..198
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT REGION 481..607
FT /note="C-terminal domain (CTD), required but not sufficient
FT to bind 70S or 30S ribosomes"
FT /evidence="ECO:0000269|PubMed:19803466"
FT BINDING 15..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT MUTAGEN 18
FT /note="K->A: No longer binds to 70S ribosomes, has no
FT GTPase activity."
FT /evidence="ECO:0000269|PubMed:18621905"
FT MUTAGEN 375
FT /note="R->A: Still binds to 70S ribosomes in presence of
FT GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 422..423
FT /note="RK->AA: Still binds to 70S ribosomes in presence of
FT GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 427
FT /note="K->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 434..436
FT /note="KGR->AGA: No longer binds to 70S ribosomes in
FT presence of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 507
FT /note="R->A: Still binds to 70S ribosomes in presence of
FT GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 509
FT /note="K->A: Still binds to 70S ribosomes in presence of
FT GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 527
FT /note="H->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 527
FT /note="H->K: Still binds to 70S ribosomes in presence of
FT GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 529
FT /note="R->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 536
FT /note="N->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 541
FT /note="K->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 542
FT /note="K->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 544
FT /note="T->P: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 547
FT /note="R->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 562
FT /note="K->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 586
FT /note="R->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP, altered secondary structure."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 588
FT /note="R->A: No longer binds to 70S ribosomes in presence
FT of GMPPNP, altered secondary structure."
FT /evidence="ECO:0000269|PubMed:19803466"
FT MUTAGEN 597..607
FT /note="Missing: No longer associates with 70S ribosomes."
FT /evidence="ECO:0000269|PubMed:19803466"
SQ SEQUENCE 607 AA; 67377 MW; 2A3ADC6F87F88B32 CRC64;
MIENLRNIAI IAHVDHGKTT LVDKLLQQSG TFDARAETQE RVMDSNDLEK ERGITILAKN
TAIKWNDYRI NIVDTPGHAD FGGEVERVMS MVDSVLLVVD AFDGPMPQTR FVTKKAFAHG
LKPIVVINKV DRPGARPDWV VDQVFDLFVN LDATDEQLDF PIIYASALNG IAGLDHEDMA
EDMTPLYQAI VDHVPAPDVD LDGPLQMQIS QLDYNNYVGV IGIGRIKRGK VKPNQQVTII
DSEGKTRNAK VGKVLTHLGL ERIDSNIAEA GDIIAITGLG ELNISDTICD PQNVEALPAL
SVDEPTVSMF FCVNTSPFCG KEGKFVTSRQ ILDRLNKELV HNVALRVEET EDADAFRVSG
RGELHLSVLI ENMRREGFEL AVSRPKVIFR EIDGRKQEPY ENVTLDVEEQ HQGSVMQALG
ERKGDLKNMN PDGKGRVRLD YVIPSRGLIG FRSEFMTMTS GTGLLYSTFS HYDDIRPGEV
GQRQNGVLIS NGQGKAVAFA LFGLQDRGKL FLGHGAEVYE GQIIGIHSRS NDLTVNCLTG
KKLTNMRASG TDEAVILVPP IKMSLEQALE FIDDDELVEV TPTSIRIRKR HLTENDRRRA
NRGQKEE
