IF2_TREPA
ID IF2_TREPA Reviewed; 842 AA.
AC O83861;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=TP_0891;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC26581.1; -; Genomic_DNA.
DR PIR; H71269; H71269.
DR AlphaFoldDB; O83861; -.
DR SMR; O83861; -.
DR IntAct; O83861; 2.
DR STRING; 243276.TPANIC_0891; -.
DR EnsemblBacteria; AAC26581; AAC26581; TP_0891.
DR KEGG; tpa:TP_0891; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_12; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000811; 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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..842
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137275"
FT DOMAIN 328..497
FT /note="tr-type G"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..344
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 362..366
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 383..386
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 437..440
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 473..475
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 337..344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 383..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 437..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 842 AA; 90925 MW; C87934788AE3C94A CRC64;
MVAKVTAARR VSCADENRTP GDASQATISA APEDKKQGFP DIREDGVARG VSASCGAVQN
AASAQVPGAR TPGVIGVPVA SKTVEEARGG GAKRVITKRV GGVFVLDDSA ARPNRKAGNL
ASGARLSRFS RSDRQRSDGF SGTQARANAG GVRRGEGRPF ARDFSRGSTG GYRPAVRGPA
RPAGRVGSGP RGPAPLQVGA GKPAQNKRSF RGRKQQTYQY QHKDRLELEE KLLQQKKKNK
EKLAAVPRSV EIMESVSVAD LAKKMNLKAS ELIGKLFGMG MMVTMNQSID ADTATILASE
YGCEVRIVSL YDETIIESVG DEHAVLRARP PVVTVMGHVD HGKTKTLDAI RSTRVAEGEF
GGITQHIGAY AVSTPKGSIT FLDTPGHEAF TMMRARGAEI TDIVVLIVAA DDGVMPQTIE
AINHAKASKV PIIVAINKID RADANPNKVM TRLAELGLAP EEWGGDTMYV SISALQGIGL
DLLLDAIMLQ AEVMELRANY GCCAEGRIIE SRIDHGRGIV ASVIVRRGVL RVGDTYVAGV
YSGRVRAIFN DQGEKIQEAT PSMPVEILGL EGMPNAGDPF QVTDSERIAR QISLKRQELR
RYENARNVKR ITLDKLYESI EKGSVSEFKV IIKGDVQGSV EALKQSLEKL STDEVQLRVI
HSSVGAINDS DVMLAAADSN VTIVGFNVRP TPQAAVLAER ERVEIKKYTV IYQAVEEMER
AMEGMLKPSL KEVVLGSAEV RKVFKIPKVG SVAGVYVLEG VMKRNAIVHV VRDGIVLHSG
KVSSLRREKD DVKEVHSGFE CGVGVENYFD FRERDRLECA EMKEVSRKLK DAALSDAARL
QG
