ID K7Y226_HELPX Unreviewed; 944 AA.
AC K7Y226;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:AFX89624.1};
GN ORFNames=HPAKL86_03070 {ECO:0000313|EMBL:AFX89624.1};
OS Helicobacter pylori Aklavik86.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055532 {ECO:0000313|EMBL:AFX89624.1, ECO:0000313|Proteomes:UP000010078};
RN [1] {ECO:0000313|EMBL:AFX89624.1, ECO:0000313|Proteomes:UP000010078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aklavik86 {ECO:0000313|EMBL:AFX89624.1};
RX PubMed=25883278;
RA Kersulyte D., Bertoli M.T., Tamma S., Keelan M., Munday R., Geary J.,
RA Veldhuyzen van Zanten S., Goodman K.J., Berg D.E.;
RT "Complete Genome Sequences of Two Helicobacter pylori Strains from a
RT Canadian Arctic Aboriginal Community.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP003476; AFX89624.1; -; Genomic_DNA.
DR RefSeq; WP_015087009.1; NC_019563.1.
DR AlphaFoldDB; K7Y226; -.
DR KEGG; hpyk:HPAKL86_03070; -.
DR PATRIC; fig|1055532.3.peg.633; -.
DR HOGENOM; CLU_006301_4_0_7; -.
DR Proteomes; UP000010078; Chromosome.
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 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 443..612
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 61..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..594
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 944 AA; 105217 MW; ECFB25283496A858 CRC64;
MSGMVDLKEF LAELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ
IQANKPTKNP EQDNKDGLNM AATPKPPNKK VSKTPKKEET KSQPKPKKTK EKKKEAPTPI
AKKKGGIEIV NTFEDQTPPI ENTPKVVSHS QVEKAKQKLQ EIQKSREALN KLTQSNANST
NSANNAKKEI SEVKKQEQEI KRHENIKRRT GFRVIKRNDE TENETENSVA ESKKPTQSVA
AIFEDIKKEW QEKDKQEAKK AKKPSKPKAT PTAKNNKSHK IDLSDARDFK GNDIYDDETD
EILLFDLHEQ DNLNKEEEEK EIRQNINDRV RVQRKNPWMN EGGIKRQSKK KRAFRNDNSQ
KVIQSAISIP EEVRVYEFAQ KANLNLADVI KTLFNLGLMV TKNDFLDKDS IEILAEEFHL
EISVQNTLEE FEVEEVLEGV KKERPPVVTI MGHVDHGKTS LLDKIRDKRV AHTEAGGITQ
HIGAYMVEKN DKWVSFIDTP GHEAFSQMRN RGAQVTDIAV IVIAADDGVK QQTIEALEHA
KAANVPVIFA MNKMDKPNVN PDKLKAECAE LGYNPVDWGG EYEFIPVSAK TGDGIDNLLE
TILIQADIME LKAIEEGSAR AVVLEGSVEK GRGAVATVIV QSGTLSVGDS FFAETAFGKV
RTMTDDQGKS IQNLKPSMVA LITGLSEVPP AGSVLIGVEN DSIARLQAQK RATYLRQKAL
SKSTKVSFDE LSEMVANKEL KNIPVVIKAD TQGSLEAIKN SLLELNNEEV AIQVIHSGVG
GITENDLSLV SSSEHAVILG FNIRPTGNVK NKAKEYNVSI KTYTVIYALI EEMRSLLLGL
MSPIIEEEHT GQAEVRETFN IPKVGTIAGC VVSDGVIARG IKARLIRDGV VIHTGEILSL
KRFKDDVKEV SKGYECGIML ENYNEIKVGD VFETYKEIHK KRTL
//
