ID A0A238J2J7_9RHOB Unreviewed; 830 AA.
AC A0A238J2J7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ECO:0000313|EMBL:SMX24928.1};
GN ORFNames=BOA8489_03061 {ECO:0000313|EMBL:SMX24928.1};
OS Boseongicola aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Boseongicola.
OX NCBI_TaxID=1470561 {ECO:0000313|EMBL:SMX24928.1, ECO:0000313|Proteomes:UP000201838};
RN [1] {ECO:0000313|EMBL:SMX24928.1, ECO:0000313|Proteomes:UP000201838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8489 {ECO:0000313|EMBL:SMX24928.1,
RC ECO:0000313|Proteomes:UP000201838};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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}.
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DR EMBL; FXXQ01000011; SMX24928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238J2J7; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000201838; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000201838}.
FT DOMAIN 328..495
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..479
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 337..344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 383..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 437..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 830 AA; 89168 MW; 00E9C8EADC03577F CRC64;
MSDNDGKKTL GLRGSRPGQV KQSFSHGRTK SVVVETKRKR VVVPKPGAAK SAGGAGGASS
PASDPSKRPA GISDAELERR MKALAAAKAV EAEEAEAREA DEKARAEDRD RRRAEAEAKE
QEEREREERA KAKAEEDERL AREAAEAKAR ADAPAVPSEP TPDAAPRSNA TKPAAAPRRD
RGDDRETRKA KPTRDDGGRR GGKLTLNQAL TGGEGGRQKS MAAMKRKQER ARQKAMGGTV
EREKVMRTVQ LPEAITVGEL ANRMSERVAD VVKSLMTSGI MATQNQTIDA DTAELIIEEF
GHKVQRVSDS DVEQVIETVK DKEEDLQDRP PVITVMGHVD HGKTSLLDAI RNAKVVAGEA
GGITQHIGAY QVEQGGNKLT FLDTPGHAAF TSMRARGAQV TDIVVLVVAA DDAVMPQTIE
AINHAKAAKV PMIVAINKID RPDANPDKVR TDLLQHEVIV EKMSGDVQDV EVSAINGTGL
DDLLEAIALQ SEILELKANP NRAATGAVIE AQLDVGRGPV ATVLVQNGTL RQGDIFVVGE
QWGRVRAMEN DHGERVKEAG PSVPVEVLGL NGTPEAGDVL NVVETEAQAR EIAEYREKAA
KDKRAAAGAA VTLDQLMANA KANEDVSELP ILVKADVQGS AEAIVQAMEK IGNDEVRVRV
LHSGVGAITE SDIGLAEASG APVIGFNVRA NAPARNSANQ KGVEIRYYSV IYDLVDDVKA
AASGLLSAEV REKFIGYAKI KEVFKVSNVG KVAGCLVTEG VARRSAGVRL LRDDVVIHEG
TLKTLKRFKD EVPEVQSGQE CGMAFENYED IRPDDVIEIF EREEVERSLK
//
