ID A0A1B7UNA6_9GAMM Unreviewed; 891 AA.
AC A0A1B7UNA6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=A5320_00525 {ECO:0000313|EMBL:OBP15961.1};
OS Rheinheimera sp. SA_1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1827365 {ECO:0000313|EMBL:OBP15961.1, ECO:0000313|Proteomes:UP000092258};
RN [1] {ECO:0000313|EMBL:OBP15961.1, ECO:0000313|Proteomes:UP000092258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA_1 {ECO:0000313|EMBL:OBP15961.1,
RC ECO:0000313|Proteomes:UP000092258};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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: 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:OBP15961.1}.
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DR EMBL; LXWK01000011; OBP15961.1; -; Genomic_DNA.
DR RefSeq; WP_068060134.1; NZ_LXWK01000011.1.
DR AlphaFoldDB; A0A1B7UNA6; -.
DR STRING; 1827365.A5320_00525; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000092258; 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; 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; 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; 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 {ECO:0000256|ARBA:ARBA00022490, 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:UP000092258}.
FT DOMAIN 391..560
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 130..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..542
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 246..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 446..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 500..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 891 AA; 97519 MW; 69B0AA70C1761E05 CRC64;
MAEVTIEKLA SDVGTTVDRL VQQFADAGIP KQTGQMVSEE EKKTLLEHLS KQHGGGSTEP
SRLTLKRKET STLSVSGGAG RNREIQVQVL KQKTYVKRPL VDDAAAAAAE EARLAEEAVK
AEEARQAAEK AAAERKIKDE ADRKADAERK ALEAKKRDEA RAQLLRDDPE EAARRQAKED
AKREADRIIA QQDAERLKKL ELDAQRQAEE ARKLAEENAE RWAKEEKAPV EVGDYHLTSN
VYAKQAEDEV DARDERGGRR HGKKAPVGKA KKKDDADDKD AFNRANRHKK KKTPTSMQHA
FNKPAQPVER EVKIGETITV AELAAKMAVK ASEVIKVMMK MGAMATINQV IDQETAAIVC
EEMGHKFTLT RENELEETVM ADREGEGQLE PRAPVVTVMG HVDHGKTSTL DYIRKAKVAA
GEAGGITQHI GAYHVETDRG MVTFLDTPGH AAFTSMRARG AKATDIVILV VAADDGVMPQ
TKEAIQHAKA AGVPLVVAVN KMDKPDADPD RVRNELSQYG VISEEWGGDT QFVPISAKTG
AGIDDLLEAI LNQAELLELK AVRQGIARGT VIESRLDKGR GPVASILVQE GTLRQGDTVL
CGFEYGRVRA MRDENGQEVK EAGPSIPVEI LGLSGVPQAG DEVTVVKDER KAREVALYRQ
GKFRDVKLAR QQKAKLENMF ANMTDGDVSE LNIVLKADVQ GSVEAISESL SRLSTEEVKI
RIIGSGVGGI TETDATLAAA SSAIIIGFNV RADATARKIV EDESLDLRYY SIIYELLDEV
RAAMTGMLAP EFKQQIIGLA QVRAVFRSPK FGAIAGCMVT EGVVKRNAPI RVLRDNVVIF
EGELESLRRI KDDVSEVRNG FECGIGVKNY NDVREGDQIE VFEVIQVVRT L
//
