ID D0YT94_9ACTO Unreviewed; 922 AA.
AC D0YT94;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:EEZ90955.1};
GN ORFNames=HMPREF0578_1958 {ECO:0000313|EMBL:EEZ90955.1};
OS Mobiluncus mulieris 28-1.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=596328 {ECO:0000313|EMBL:EEZ90955.1, ECO:0000313|Proteomes:UP000005581};
RN [1] {ECO:0000313|EMBL:EEZ90955.1, ECO:0000313|Proteomes:UP000005581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-1 {ECO:0000313|EMBL:EEZ90955.1,
RC ECO:0000313|Proteomes:UP000005581};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (NOV-2009) 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:EEZ90955.1}.
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DR EMBL; ADBR01000033; EEZ90955.1; -; Genomic_DNA.
DR AlphaFoldDB; D0YT94; -.
DR eggNOG; COG0481; Bacteria.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000005581; 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}.
FT DOMAIN 416..590
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 61..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 475..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 529..532
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 922 AA; 98219 MW; 409FC0E4ECA4F8C6 CRC64;
MARMRVHELA KKLGTDSKTM LDVLKDAGEF VKSASSVVES PVVKKITKHF EEKKLGKFSP
EAAKKAAKAA EKAAADITKK PTVAPAMTDT TAVDTVETEE VRDEGASEPK REAPHEVGET
PSVEAEAAEK TPESTPPAAT PIETTPTAPV PTPSAKPTAP NTSAPGRAIP KPGARMPKPG
QVRPGNNPFA SSQGMPRPGG TGGVKPGSRR GRPGNNPFAS AQGMPRPASG GARPKPGDHA
RGAGDGQGNA PSHPGRGGRG GHGGDSQRNF AAPPTNRGRG GRGSTQGAFG RGKSKKSKAR
REKRQEIEEQ SAPVIGGVSI PKGNGEEIRI RSGASLADFA EKIHVNPAAL VTVLFHMGEM
ATANQSLDED TFKLLGTELG YDITIVSPED EDRDILESFD IDLEAEELDD IDSLETRPPV
VTVMGHVDHG KTKLLDAIRN TDVVEGEYGG ITQHIGAYQV TLKKADKGRR ITFIDTPGHE
AFTAMRARGA EVTDIAIIVV AADDGVMPQT VEAINHAKAA EVPIVVAVNK IDKPEANPDK
VKAQMSEYGV LPEEYGGDTM FVEISAKQRQ GITELLDAVL LTADAVLELK ANPDAPARGV
AIEANLDKGR GAVATVLVQR GTLRVGDAIV AGTAYGRVRA MFNERGQNVD EAGPSTPVQV
LGLTSVPRAG DSFLVAEDDR TARQIADKRA AVERAALLAK RRKRVTLESF DEALKAGKVD
MLNLIIKGDV SGSVEALEDS LLKIDVGDEV GLRIIHRGVG AITQNDVNLA TVDNAVIIGF
NVRPAERVAE YADAQGVDMK FYSVIYQVIE DVENSLKGML KPIYEEHDLG SAEILQVFKS
SKFGNIAGCI VKSGTIKRGT KARLVREGVV VNQELSIHSL RREKDDVTEV REGFECGIGL
DFKDIQVGDR IETWEMKEIP RN
//
