ID I9NS54_9FIRM Unreviewed; 843 AA.
AC I9NS54;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=JBW_02341 {ECO:0000313|EMBL:AJQ27687.1};
OS Pelosinus fermentans JBW45.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1192197 {ECO:0000313|EMBL:AJQ27687.1, ECO:0000313|Proteomes:UP000005361};
RN [1] {ECO:0000313|EMBL:AJQ27687.1, ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|EMBL:AJQ27687.1,
RC ECO:0000313|Proteomes:UP000005361};
RX PubMed=26404608;
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Elias D.A., Arkin A.P.,
RA Fields M.W., Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45, a Member of a
RT Remarkably Competitive Group of Negativicutes in the Firmicutes Phylum.";
RL Genome Announc. 3:e01090-e01015(2015).
RN [2] {ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|Proteomes:UP000005361};
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Arkin A.P., Fields M.W.,
RA Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45.";
RL Submitted (FEB-2015) 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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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; CP010978; AJQ27687.1; -; Genomic_DNA.
DR RefSeq; WP_007956396.1; NZ_CP010978.1.
DR AlphaFoldDB; I9NS54; -.
DR STRING; 1192197.JBW_02341; -.
DR KEGG; pft:JBW_02341; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000005361; 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; 1.10.10.2480; -; 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; 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; 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; 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:UP000005361}.
FT DOMAIN 343..510
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 53..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..494
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 53..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 452..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 843 AA; 92501 MW; 93A995A078C91A7B CRC64;
MSKYRIYELA KDFNTTSKVI IDILNRNNME AKNHMSSVDD DAKNVITRTF AHKITSTPTS
GTSTIENKPR TQEQPTQTTR SLGSDGRQQP LSNSGEQRPA SNPQPQRSWQ NQSNQNRPQQ
NQQRPPQVPF QGQRPPQAPF QGQRPPQNTQ NQQRPPQAPF QGQRPPQNTQ NQQRPPQAPF
QGQRPPQQNF QPRNAGTQQP PVQSRPAAPP NKFQSNNNRS TNNNNAQRNQ GGGNFNRRPQ
ANRGFQSRGA APAVKIEPPK PKSVKLGESI TVKELSSKLC RDVGEVIKKL MMLGVMATIN
QDLDFETASL LATEFGVEVL ELPPEEDPTE IAEIEDDPSS LVLRPPVVTV MGHVDHGKTS
LLDSIRQTHV TSQEAGGITQ HIGAYKVTCQ GKKIVFLDTP GHEAFTAMRA RGAQVTDIAI
LVVAADDGVM PQTIEAINHA KSANVPIIVA INKMDRPGAN PDRIKQQLSD YGLVAEDWGG
EAIMVPVSAQ KKTGINELLE MILLVAEMQE IKANPNRQAY GTIIEAKLDK GRGPVATVLV
QKGTLHIGDT IIAGIAYGKV RAMVNDRGEK VKKAEPSTPV EVLGLADVPQ AGDVLVAVDE
KIARAVAEKR IAKRRTDELM QSQKVSLDDL FKQIQDGNIQ DLNIVIKADV QGSVEALRQS
LLALNANNKE VRVNIVHAGV GAINESDVML ASAANALIIG FNVRPDGNAR KAGESEKIDI
RLYRVIYEAL HDVEAAMTGM LAPEYKEALQ GRVEIRQLFT ISKVVIAGAY VLEGKILNSS
QVRVIRNGIV IHEGELESLR RFKDDVKEVA AGYECGITID KFRDIKEGDI IEAFTMEEIK
PKG
//
