ID J0LGZ3_HELPX Unreviewed; 949 AA.
AC J0LGZ3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:EJB61780.1};
GN ORFNames=HPHPH41_0481 {ECO:0000313|EMBL:EJB61780.1};
OS Helicobacter pylori Hp H-41.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992046 {ECO:0000313|EMBL:EJB61780.1, ECO:0000313|Proteomes:UP000003606};
RN [1] {ECO:0000313|EMBL:EJB61780.1, ECO:0000313|Proteomes:UP000003606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp H-41 {ECO:0000313|EMBL:EJB61780.1,
RC ECO:0000313|Proteomes:UP000003606};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
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:EJB61780.1}.
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; AKOM01000002; EJB61780.1; -; Genomic_DNA.
DR RefSeq; WP_001282232.1; NZ_AKOM01000002.1.
DR AlphaFoldDB; J0LGZ3; -.
DR PATRIC; fig|992046.3.peg.466; -.
DR Proteomes; UP000003606; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}.
FT DOMAIN 448..617
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 64..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..599
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COILED 310..340
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 91..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 503..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 557..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 949 AA; 105949 MW; A98CE2AA98CFED30 CRC64;
MSDMVDLKKF VTELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ
IQANQPAKNL EQDNKDDLKI AATPKPLAKK ASKTPKKEET KAQPKPKKTK EKKKEAPAPI
IKKKGIEIVN TFENQTPPVE NTPKVVSHSQ IEKAKQKLQE IQKSREALNK LTQSNTNTTN
NANNASNTNN AKKEISETKK QEQEIKRHEN IKRRTGFRVI KRNDEVENET ENSVTESKKP
TQSVAAIFED IKKEWQEKDK QETKKPKKPS KPKATPTAKN NKSHKIDFSD VRDFKGNDIY
DDETDEILLF DLHEQDNLNK EEEEKEARQN INDRVRVQRK NPWMNEGGIK RQSKKKRAFR
NDNSQKVIQS AIAIPEEVRV YEFAQKANLN LADVIKTLFN LGLMVTKNDF LDKDSIEILA
EEFHLEISVQ NTLEEFEVEE VLEGVKKERP PVVTIMGHVD HGKTSLLDKI RDKRVAHTEA
GGITQHIGAY MVEKNNKWVS FIDTPGHEAF SQMRNRGAQV TDIAVIVIAA DDGVKQQTIE
ALEHAKAANV PVIFAMNKMD KPNVNPDKLK AECAELGYNP VDWGGEHEFI PVSAKTGDGI
DNLLETILIQ ADIMELKAIE EGSARAVVLE GSVEKGRGAV ATVIVQSGTL SVGDSFFAET
AFGKVRTMTD DQGKSIQNLK PSMVALITGL SEVPPAGSVL IGVENDSIAR LQAQKRATYL
RQKALSKSTK VSFDELSEMV ANKELKNIPV VIKADTQGSL EAIKNSLLEL NNEEVAIQVI
HSGVGGITEN DLSLVSSSEH AVILGFNIRP TGNVKNKAKE YNVSIKTYTV IYALIEEMRS
LLLGLMSPII EEEHTGQAEV RETFNIPKVG TIAGCVVSDG VIARGIKARL IRDGVVIHTG
EILSLKRFKD DVKEVSKGYE CGIMLENYNE IKVGDVFETY KEIHKKRTL
//
