ID A0A0K2LCY0_9LACO Unreviewed; 986 AA.
AC A0A0K2LCY0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ORFNames=JP39_06580 {ECO:0000313|EMBL:ALB29053.1};
OS Companilactobacillus heilongjiangensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1074467 {ECO:0000313|EMBL:ALB29053.1, ECO:0000313|Proteomes:UP000061546};
RN [1] {ECO:0000313|EMBL:ALB29053.1, ECO:0000313|Proteomes:UP000061546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28069 {ECO:0000313|EMBL:ALB29053.1,
RC ECO:0000313|Proteomes:UP000061546};
RA Jiang X., Zheng B., Cheng H.;
RT "Genomic sequence of Lactobacillus heilongjiangensis DSM 28069, isolated
RT from Chinese traditional pickle.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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; CP012559; ALB29053.1; -; Genomic_DNA.
DR RefSeq; WP_041501778.1; NZ_CP012559.1.
DR AlphaFoldDB; A0A0K2LCY0; -.
DR STRING; 1074467.JP39_06580; -.
DR KEGG; lhi:JP39_06580; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000061546; 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; 1.10.10.2480; -; 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; 2.
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 487..656
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 34..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..638
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 90..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 496..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 542..546
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 596..599
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 986 AA; 109062 MW; CEFEA75CAA4DFEE1 CRC64;
MVKKRIYTIA KENSVENQVV LDAASKLGID VKNHMSSVDE GAEKKIVSNL KGGKPAPAKA
ASKPVTRPAA KPASKPATHQ TQSSRPAQPA KAGEKHEGSN HNSGDHKTKI KITAVRRDAN
KGNGHFDHRN NNHTSNGNRP NSNNSNTNHR NNNTTANANS NNRSDNRNTP SRDNRSNDNR
NNNGNRNNNT NNRNNNNRNS QSRDNRNRNN NRRDRSNGTQ SQAPRPTQSA GNKYLEQFKT
NIADASRIPS HPTRNNNNRP NNRNNSSDNT HRNNQNNHRP NNNNGENQSR FNRNNNNNHN
NTNSNNRNNN SQNNNQNRRP NNNNNVAAKA KETPKSTVAH VEVPKPEYKK AKPTNNNRDF
GHKTNLANPF GSRRKKKERK RQQRQRTEPK KPMPQRKERP LPETLTYTVG MNAQDIGKLL
HREPAELVKK LFMLGIMINQ NKSLDKDTIE LLAEDYGIKA EEKVQEDVAD IDKYFDAEAN
NADNLVTRPP VVTIMGHVDH GKTTLLDHLR HTHVTAGEAG GITQHIGAYQ VRLKDRLITF
LDTPGHAAFT NMRARGADIT DIVILVVAAD DGVMPQTIEA INHAKAANDP IIVAINKIDK
PGANPQHVTE ELMKYDLVPE SYGGDTIFVN ISAKMGTNID ELLEMILLES DVLELKANPE
QKAIGTVIEA KLDKGRGPVA TLLVQQGTLH VGDPIVVGNT FGRVRTMTNY NGKDIEAAKP
SEPVEVTGLN DVPESADKFV VFDDEKTARA AGEERASRAL QKERQNTNPV TLDNLFETMK
EGELKQVDVI IKADVQGSAE AIAGSLKKIE VKGVRVNIIH SAVGAITESD VNLASASNAI
IIGFNVRPTA QAKVQAKDEN VDIRLHRVIY KAIDEIEAAM KGMLEPVYEE KITGNLTVRE
TYNVSKIGTI AGCYVDSGKI QRDSGVRLVR DGVVVYEGKL ASLKRFKDDV KEVGSGFECG
ITIENYNDIK IGDEVEAYVM EEVPVK
//
