ID IF2_AZOSB Reviewed; 940 AA.
AC A1K7B9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=azo2107;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; AM406670; CAL94724.1; -; Genomic_DNA.
DR RefSeq; WP_011765838.1; NZ_CP016210.1.
DR AlphaFoldDB; A1K7B9; -.
DR SMR; A1K7B9; -.
DR STRING; 62928.azo2107; -.
DR KEGG; aoa:dqs_2239; -.
DR KEGG; azo:azo2107; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000002588; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 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; SSF46955; Putative DNA-binding domain; 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; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..940
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335458"
FT DOMAIN 440..609
FT /note="tr-type G"
FT REGION 138..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..456
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 474..478
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 495..498
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 549..552
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 585..587
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 146..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 495..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 549..552
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 940 AA; 100829 MW; 75C673CB04A9D1B4 CRC64;
MEQMSVTQFA GELKMPAAAL LEQLKRAGVD KSSAADLLTE QDKSRLLEYL RRAHGGGEPK
GKITLTRKQT TEIRATDSTG RARTVQVEVR KKRTFVKRDE LLGDAASAES PLLEEELSVA
GEAAGEAVAA PEPVLEAAPV EVVAEPEPVQ PEPLPEPEPE PVVVEEAPVQ QAAEPEPVEA
AAVAAEAESP ESAQPAAPRA RPVSITELLS EEEIAARERE ARRHRELVER QQADLRARQQ
REAAAKAAAE ARRLDEEAKA RAEQQKKEEA AKPAAKPAPG PTGTLHRPAK ADDKAGKDAK
RGPAREADGA KRRGIKTRGE VGGAASGNAW RGAKGGGRHG RQQDDRQTFQ APTEPIVREV
HVPETITVAD LAHKMSVKAT EVIKTLMKMG SMVTINQVLD QETAMIVVEE LGHKALAAKL
DDPDAFLEET DAHKDAELLP RAPVVTVMGH VDHGKTSLLD YIRRAKVAAG EAGGITQHIG
AYHVETPRGV ITFLDTPGHE AFTAMRARGA KATDIVILVC AADDGVMPQT REAIHHAKAA
GVPVVVAITK IDKPEANAER VKQELVSESV IPEEYGGDTM FVPVSAKTGT GVDELLEAVL
LQAEVLELTA AVDAPAKGLI VEARLDKGRG PVASLLVQSG TLRKGDVLLV GATFGRIRAM
LDENGKPVDE AGPSIPVEIL GLSDVPAAGD EAIVLGDEKK AREIALFRQG KFRDVKLAKQ
QAAKLESMFE QMAEGEVKSL PLIIKADVQG SQEALAQSLA KLSNDEVRVN VIHGAVGAIS
ESDVNLAQAS GAVIIGFNTR ADAGARKLAE SFGVDIRYYN IIYDAVDEVK SALSGMLAPE
KREEVIGMVE IRQVFTISKV GSVAGCYVLE GLVKRGSSVR LIRNHTVVWT GELESLKRFK
DDVKEVKFGY ECGLQLKNYN DIQVGDQLEV FEIKEVARTL
//
