ID W2VIA5_9FIRM Unreviewed; 970 AA.
AC W2VIA5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:ETO97183.1};
GN ORFNames=HMPREF1495_2537 {ECO:0000313|EMBL:ETO97183.1};
OS Lachnoanaerobaculum sp. MSX33.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936596 {ECO:0000313|EMBL:ETO97183.1, ECO:0000313|Proteomes:UP000018910};
RN [1] {ECO:0000313|EMBL:ETO97183.1, ECO:0000313|Proteomes:UP000018910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSX33 {ECO:0000313|EMBL:ETO97183.1,
RC ECO:0000313|Proteomes:UP000018910};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (DEC-2013) 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}.
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:ETO97183.1}.
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DR EMBL; AZXX01000062; ETO97183.1; -; Genomic_DNA.
DR RefSeq; WP_034212991.1; NZ_AZXX01000062.1.
DR AlphaFoldDB; W2VIA5; -.
DR PATRIC; fig|936596.3.peg.1221; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000018910; 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; 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}.
FT DOMAIN 470..639
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..621
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 51..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..486
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 525..529
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 579..582
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 970 AA; 106711 MW; F7B732A138EBE865 CRC64;
MRVNDLAKEL GKNNNELTAY LKENGISKVA MSNISADEEK MLREKFNKID GNKVVNNNKE
NMENNRTVET TQEVSETKKE EAPKKKVVVF RPQNAQQMPA KKSGSKSAQA PKKNTKKDAE
ATKQPQKKAT EEKKTDISKS DISKEIKKEE KAVETVKTEE VVTAKEPVAN VESKTPVATE
EKKAQAPVLE SAEPAKPRNV YAEMEAAKKA KESAQPIRNI FKEREERDKA RGKDSRPQNR
DKKPFNKDKD QKGNFKNDRN SKVRDGAGNN DRNRNFAGKD NKNFQGSNDR NNRNDRNKDF
SKDENTGRSF GNNKQQGFKK NDAAAGVPVL DGLGKKTSNR VNKNNFKNNN KNDKKHRTED
GPAKGKVSKH PFIMPVKQKV EEVQDDIKEI IIPETITIKE FASKLKLQPS TIVKKLFLKG
QIVTLNTELT FEQAEEIALE YDVICTMEEK VDVIGELLAE AEDPEETLVS RPPVVVVMGH
VDHGKTSLLD AIRKTNVTSR EAGGITQHIG AYMVKINGEP ITFLDTPGHE AFTAMRMRGA
QATDIAILVV AADDGVMPQT VEAINHAKAA GVEIIVAINK IDRPAANIDK VKQELSEYEL
IPEDWGGSTI FVPVSAKNGD GISNLLEMVI LTAEVKELKA NPNRKARGLV IEAELDKGKG
PVARILVQKG TLHVGDFIAA GSCSGKVRAM MNDKGVKVKS AGPSTPVEIL GLDSVPNAGE
VFVATENDKE AKAFAATFIS ESKNKLIEDT KAKLSLDDLF SQIKAGNVKE LPIVVKADVQ
GSVEAVKQSL TKLSNEEVAV KVIHGGVGAI NESDVVLAAA SNAIIIGFNV KPDQMAKATA
ERENVDLRLY RVIYQAIEDI ESAMKGMLEP IYEEKVIGHA EIRQIFKASG VGNIAGSYVL
DGKFVRGCKV RITRDGEQIF DGNLASLKRF KDDVKEVATG YECGLVFEKF NDIKEFDQVE
AYAMVEVPRS
//
