ID   IF2_ALTMD               Reviewed;         868 AA.
AC   B4RXT8; F2GAC8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=MADE_1008920;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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}.
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; CP001103; AEA97922.1; -; Genomic_DNA.
DR   RefSeq; WP_012518253.1; NC_011138.3.
DR   AlphaFoldDB; B4RXT8; -.
DR   SMR; B4RXT8; -.
DR   GeneID; 56342192; -.
DR   KEGG; amc:MADE_1008920; -.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   Proteomes; UP000001870; 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.
FT   CHAIN           1..868
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093755"
FT   DOMAIN          368..537
FT                   /note="tr-type G"
FT   REGION          49..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..384
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          402..406
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          423..426
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          477..480
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          513..515
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        92..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         377..384
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         423..427
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         477..480
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   868 AA;  95580 MW;  32AA374822B8D3FD CRC64;
     MADVSIEKLA SDIGTTVDRL VGQFKDAGIS KSAGEQVNED EKQKLLDHLS KQHGSAAEPT
     RMTLKRKTTS TLSVGKSKEV KVEVRKKRTY VKRSDIEEQQ RQAEEEAKRL EEEARLKREA
     EEKAAAEAKK AAEEKARKAQ EAKKAAEEER VRRAEQAKKE AEARKKDEPE LTEAEKAEAE
     AARQEEERLR KAQEEEAQKK LEEDAKKAAD EARKLAEENE RRWKEEEERR KKAEAEEVHL
     HSNRYAQEAE DEEDMQVERS SRRRRKSKKN AGEHLKQGFN KPAAPVERVV KLGATITVGE
     LASKLAIKSN EVIKTMMKMG EMATINQVLD QDTAVLVIEE MGHKYELVND NALEDELLAD
     GTDGEKTSRA PVVTIMGHVD HGKTSLLDYI RRAKVADGEA GGITQHIGAY KVQTDNGEIT
     FLDTPGHAAF TAMRARGATA TDIVILVVAA DDGVMPQTKE AVQHARAAGV PLIVAVNKMD
     KETADPDRVK TELSQLEVIS EEWGGEHQFC NVSAKTGMGV DELLEAIVLQ SELLDLQAVA
     EGPGRGIVIE SRLDKGRGPV ASVLVQEGQL RAGDILLCGE EYGRVRAMRD ENGKDMKLAG
     PSTPVEVLGL SGVPVAGEDA AVVKDERKAR EVAAKRHQKK RELKLARQQK AKLENMFANM
     ESGDVSELNI VLKADVQGSV EAISESLIKL STSEVKVNIV GSGVGGITET DATLAAASGA
     IVLGFNVRAD ATARRVLEAE EIDLRYYSVI YNLIDEVKAA MSGMLAPEFK QEIIGLAEVR
     DVFKSPKLGA IAGCMVTEGN VKRSNPIRVL RDNVVIYEGE LESLRRFKDD VQDVRNGMEC
     GIGVKNYNDV KVGDQIEVFE IVEVKREI
//