ID V9TRV9_9PROT Unreviewed; 872 AA.
AC V9TRV9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:AHC73296.1};
GN ORFNames=P856_46 {ECO:0000313|EMBL:AHC73296.1};
OS Candidatus Endolissoclinum faulkneri L5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Endolissoclinum.
OX NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73296.1, ECO:0000313|Proteomes:UP000018700};
RN [1] {ECO:0000313|EMBL:AHC73296.1, ECO:0000313|Proteomes:UP000018700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=faulkneri L5 {ECO:0000313|Proteomes:UP000018700};
RX PubMed=24324632;
RA Kwan J.C., Schmidt E.W.;
RT "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT conservation of secondary metabolism.";
RL PLoS ONE 8:E80822-E80822(2013).
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}.
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DR EMBL; CP006745; AHC73296.1; -; Genomic_DNA.
DR AlphaFoldDB; V9TRV9; -.
DR STRING; 1401328.P856_46; -.
DR KEGG; efk:P856_46; -.
DR PATRIC; fig|1401328.3.peg.46; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR Proteomes; UP000018700; 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: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:UP000018700}.
FT DOMAIN 361..529
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 370..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 417..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 471..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 872 AA; 96345 MW; DE25CEB63474C475 CRC64;
MDDVRKDNMS SSKEEDRKKL SLASNKETLS IGKSMETAQV KQSFSHGRSK TVQVEVRRRR
MFNTPSASPH KGKSRIGRQS DRELTAEERE VRSRILEQAT IKRPENQLDV VNKVKLPTEP
DVNILTKPSK IVTAQSDIAP ISRRQTEMDE LRKIKDTEAA IRAIETSRIA EGEANRQAKA
AAERATARLN RETTVATEID DESKRKRGGS NKESSTKRSS SRTRSGGAER SRRRQGKLTI
TDALSEDSWR MRSLASVRRA RERERKRGRS NPGESIRQSR DVIVPETITV QELANRMAER
GGDVIKTLMK MGFLATINQM LDADTAELVA QTLGHKVRRV AESDVELGMA GEEDSYADLQ
PRPPVVTVMG HVDHGKTSLL DAIRQADVAS SEAGGITQHI GAHQIELPSR DKITWIDTPG
HESFTEMRAR GANVTDIVLL VVAADDGIMA QTIEAIRHAK AANVPIIVAV NKIDKPEADP
ERVRTDLLQH AIVVEDMGGD VQAVDVSAQT KHGLSVLLEA IIVQAEILEL KANPNRAASG
IVIEAKVERG RGSVATVLVQ RGTLRTGNVF VAGAEWGRVR ALINDRGKSA EIAIPSDPVE
VLGLQGTPIA GDDFVVVENE NRAREIANYR RRRLREKSAT VGNRSTVEQM LSAIKSSEAA
ELPLVLKADV HGSLEAIRAS IEKMENRLVK PRILHAAVGG ISESDVSLAR ASSAIVVGFN
VCANPQAREM ARLDGMELRY YSIIYDLIDD MKTLLTGMLA PELNEEFLGY AEIRQIFDIT
KVGKVAGCMV REGVIKRACK IVRLIRDNVV IHEGSMKTLK RFKEEVREVR EGYECGIAFE
SYDDIREGDQ IQCLDLKEVA RTLEQVQQQT SA
//
