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Database: UniProt
Entry: A0A2A8HZA2_9SPHN
LinkDB: A0A2A8HZA2_9SPHN
Original site: A0A2A8HZA2_9SPHN 
ID   A0A2A8HZA2_9SPHN        Unreviewed;       872 AA.
AC   A0A2A8HZA2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=B2G71_01990 {ECO:0000313|EMBL:PEQ14391.1};
OS   Novosphingobium sp. PC22D.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1962403 {ECO:0000313|EMBL:PEQ14391.1, ECO:0000313|Proteomes:UP000220675};
RN   [1] {ECO:0000313|EMBL:PEQ14391.1, ECO:0000313|Proteomes:UP000220675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC22D {ECO:0000313|EMBL:PEQ14391.1,
RC   ECO:0000313|Proteomes:UP000220675};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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|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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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:PEQ14391.1}.
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DR   EMBL; MWMO01000001; PEQ14391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8HZA2; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000220675; 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; 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; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000220675}.
FT   DOMAIN          370..540
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..86
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         379..386
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         426..430
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         480..483
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   872 AA;  93816 MW;  982DF658F44DB031 CRC64;
     MSETDNKPTL GRKPLGLKRS VEAGEVKQTF SHGRTNKVVV EVKRRKLIGK PGAEAASEAA
     PAAEKPAPEA KKSAPPPAPA PKKPAPKKAA PSGETPQERV ARLQREAEEE RLRLTEEARR
     REDEAKAREL EEEKRRAEEN RRAEEEAAKA EQAAAAAEKQ AAEAATGTPA PAPAEAPAPA
     SPAAEAAPAD DAEAPAPRRF TPVARPEPKK AEPVTAKKPA DGGKKASANR GADRKGGDRR
     RDGKLTVTRA LNDDEGARAR SLAALKRARE KERRAHFTGR SQPREKQVRD VVVPEAITVQ
     ELANRMAEKG ADLVKALFNL GMMVTVNQTI DQDTAELLVE EFGHNITRVS ESDIDIDTSG
     DVDADETLKP RPPVVTIMGH VDHGKTSLLD ALRGTDVVRG EAGGITQHMG AYQIKTKGGD
     LVTFLDTPGH AAFTAMRARG ANVTDIVVLV VAADDGIMPQ TVEAINHTKA AGVPMIVAIN
     KVDKPEANVK KVRERLLEHE VIVEELSGDV QDVEVSAKTG KGLDELIEKI LLQAEFLELK
     ANPDRDAEAT VIEAKLDKGK GPVATVLVTR GTLKRGDVFV VGTQSGRVRA MNDDKGRQVK
     EAGPAMPVEV LGLGGVPMAG DLLSVVENEQ RAREVSEYRQ EQATAKRTAM APASLDTMFS
     ALADKQNVIE YPVVIKADVQ GSIEAINNAL HNLSNDEIKV RILHSGVGAI TETDVTLASA
     SNAPIVGFNV RPNAKARQQI EQTKTPMLYY DVIYELTEEI AKQMAGIWGP ERVETVVGRA
     EVKQVFPAGK KDKAAGLLVV EGAIRKGLHA RLTRNDVIVS ATTIASLRRF KDDVDEVRTG
     LECGVVLADT NDIRAGDQLE VFEVSERERT IG
//
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