IF2_RHOBA
ID IF2_RHOBA Reviewed; 1038 AA.
AC Q7URR0;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RB5504;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; BX294142; CAD74278.1; -; Genomic_DNA.
DR RefSeq; NP_866738.1; NC_005027.1.
DR RefSeq; WP_011120484.1; NC_005027.1.
DR AlphaFoldDB; Q7URR0; -.
DR SMR; Q7URR0; -.
DR STRING; 243090.RB5504; -.
DR PRIDE; Q7URR0; -.
DR EnsemblBacteria; CAD74278; CAD74278; RB5504.
DR KEGG; rba:RB5504; -.
DR PATRIC; fig|243090.15.peg.2647; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR InParanoid; Q7URR0; -.
DR OrthoDB; 138372at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; 2.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1038
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137242"
FT DOMAIN 529..696
FT /note="tr-type G"
FT REGION 32..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..545
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 563..567
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 584..587
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 638..641
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 674..676
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 207..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 538..545
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 584..588
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 638..641
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1038 AA; 110115 MW; 82608B839C94D48A CRC64;
MPVRIYALAK ELNLDSKELV DVVKKAGITG KGSALASLSD EEAQQVRGHL AGSAAKSEPK
PKAAPPTKDT PTAPVAPVRD LSGATGRKPS AINVGRPSKP AEAADNPNAP AQPIRDGGRP
VGKPAPIVRT PKLAPAPEAK APEAPAADGS PKPEIRLPKT GGVGTGMASP SGRGIGMGAK
TDGQSTKPES AASAPSVPGP KSDSGGRKAP ESPKRESAPV ASSDDDGSSN KGGGLASRIA
GRMGNNSSGR VVPNTPGTPL SAVRRDSASA GGKMRSLDRS RNRPEEAAKA GDAGKSKKRE
PRIKVNLAQL PSAPAKPAAP TGSSGPAAQK PDIKLTRDVI EGHKQGMKAP LARLEQDEAD
KKQRSKKTAE GTVGLAGRGK RVIDEDEKPK KKGLAGMASA RAERQRGGGG RRIVGSDGGD
RHHYRRSRPR IRRKGVNTAA PRKEKVQIEL PCTVRNFCEG SGLSVADVMR TLMGMGMMVN
INADIDFETA ELLATEHDLD IELKAAESLE QELITEIEET ADDPDTLVAR PPVVTFLGHV
DHGKTSLLDH LVGINVVKGE AGGITQHIRA YKIDKDGRAV TFVDTPGHEA FTEMRARGAN
VTDIAVLVVA ADDGIMPQTE EAISHAKAAE VPIVVALNKI DLEGVDANRV MTQLTEHQLT
PSEWGGDVEI VRTSATQGTG MDELLDTLLT IAELNEYSAN PNRSALGVCL ESEQQGDRGV
VAKLIVQNGT LRVGDILVCG PAHGRVRAMQ DTLTGKPITE AGPSTPVSLM GLDTPPGAGD
RFHVLKDISQ AREIASAREG ESSRQSLSGI TTKVSFDSFQ EMLEDGKLGE SADTVKLNLI
IRADARGSLE AIDKELSKFD HPEVEIRVLQ RSVGGISLAD ATLASASDAV ILGFNVIPDD
KARSLAEERG VEIRRYDVIY KLTDDIRALI EGRLKPEERV VELGRALVKQ VFSISRVGTI
AGCYVAQGSI QRNCRIRVNR DGRTIGDYQL DTLRRIKEDV KEVPRGMECG IRLQGFNDIK
QDDVLEAYKI EEVARKLD
