ID A0A0W1KMF7_9ACTO Unreviewed; 912 AA.
AC A0A0W1KMF7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:KTF04766.1};
GN ORFNames=AQZ59_00066 {ECO:0000313|EMBL:KTF04766.1};
OS Trueperella bernardiae.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF04766.1, ECO:0000313|Proteomes:UP000054404};
RN [1] {ECO:0000313|EMBL:KTF04766.1, ECO:0000313|Proteomes:UP000054404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF04766.1,
RC ECO:0000313|Proteomes:UP000054404};
RA Bernier A.-M., Bernard K.;
RT "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT 0504T, Isolated from Blood Culture.";
RL Submitted (NOV-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|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}.
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:KTF04766.1}.
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DR EMBL; LNIZ01000001; KTF04766.1; -; Genomic_DNA.
DR RefSeq; WP_062612084.1; NZ_LNIZ01000001.1.
DR AlphaFoldDB; A0A0W1KMF7; -.
DR STRING; 59561.AQZ59_00066; -.
DR PATRIC; fig|59561.3.peg.66; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000054404; 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 PRINTS; PR00315; ELONGATNFCT.
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:UP000054404}.
FT DOMAIN 405..579
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 464..468
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 518..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 912 AA; 97158 MW; 16E1033F3C37E6D9 CRC64;
MAKVRVHELA KEIGVTSKRL LEVLKESGEF VTSASSSIEA PVVRKAREYF DKHPEDVKKP
SGKGAKKAPA KAQAAPAASA TSDKQEAQPA AKSAPTPAAM ASKSSDKPAP GPRVADENKD
AAQEAPEAKA AEPKATPASA NKRTIATPGE AARSAQAARD AAPPRPQPRR GGPRPGNSPF
ASKQGMGRPR PGNSPFAPKQ GMRSDSAKKT PKPAGGPRPS PNMMPEHIKT DANRSRGRGR
PATTGGNTFG TSNNQRGGGF VRSGGKARGG STAGAFGKRN GGSRRKSKRM KRQEWEEQQN
PMVAGISVPR GNGQTVRVRA GSSLADFAER IDADPAALVT VLFRMGEMAT ANQSLDEDTF
QLLGAELGYD IKIMSPEDED REILEAFDID LEAEREETDP EDLLPRPPVV TVMGHVDHGK
TKLLDAIRNE DVALGEAGGI TQNIGAYQTH VDVEGERRSI TFIDTPGHEA FTQMRARGAD
VTDVAILVVA ANDGVMPQTV EAINHVQAAD VPIVVAVNKI DVDGANPAKV RAQLTEYGLV
AEDYGGDVPF VDISAKQRIN IGELLSTVVA TSDILVEPKA DPDKAARGVA IEAKLDQGRG
SVITALIQDG TLHIGDSIVV GTAYGRVRAM IDEHGNNVDE AGPSRPVQVL GLTSVPGAGD
QLIVADDDRT ARQIAERREA AKRAATLAKR RKRISLEDLT AAIEEGKVET LNLIIKGDSS
GSVEALEASL LEIEVGQGEV ELQVIHRGVG AVTQSDVDLA TVDNAVIIGF NVRPAERVQE
LADQEGVEMK FYNVIYSAID EVEAALKGKL KPIYEEVEVG TAEIRQVFRS GKFGNIAGSI
VRSGTINRGH KARLVRDGVV VAPELTIESL RREKDDVTVV REGYECGITL GFNDIAEGDI
IETWEMREKP RD
//
