IF2_NITOC
ID IF2_NITOC Reviewed; 845 AA.
AC Q3J9B6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Noc_2120;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA58580.1; -; Genomic_DNA.
DR RefSeq; WP_011330866.1; NC_007484.1.
DR AlphaFoldDB; Q3J9B6; -.
DR SMR; Q3J9B6; -.
DR STRING; 323261.Noc_2120; -.
DR PRIDE; Q3J9B6; -.
DR EnsemblBacteria; ABA58580; ABA58580; Noc_2120.
DR KEGG; noc:Noc_2120; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006838; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF46955; SSF46955; 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..845
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228218"
FT DOMAIN 345..512
FT /note="tr-type G"
FT REGION 139..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..361
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 379..383
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 400..403
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 454..457
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 490..492
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 139..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354..361
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 400..404
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 454..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 845 AA; 92578 MW; 7898CBA56B1106FE CRC64;
MSEVTVRQLA DVVGTPVGRL LEQLREAGIG VDREDAAITE AQKLQLLRYL RHSHGASVEI
ATPKRITLNR RSHSEIQVNA GGGRSKTVNV EVRKKRTYIK RSAILEQERL AERQREEEEA
QAGVQAQQER EARLIAEEEA KRQAAEEEAK RQAAEEEAKR QAAEEEAKRQ AEAQVKRRLD
VEKKPKNGLE PARTEKPASR KAKPRFRSED RESEQKQRGT KFGRKELHIA PGKAGTSKRK
KFRPQKAAPA AKHGFERPTA PIVHDVSIPE TMTVAELAQK MSVKAAEVIK ALMKLGIMAT
INQVLDQDTA TIVVEEMGHK PKRLQENTLE LELVQAEQEV SRQVSRAAVV TIMGHVDHGK
TSLLDYIRRA KVATSEAGGI TQHIGAYKVR SDKGEITFID TPGHAAFTAM RARGAKVTDI
VILVVAADDG AMPQTVEAIQ HARAAGAPLV VAVNKIDRPD ADPDRVKQEL ANHDVITEEW
GGDTQFVNVS AKTGEGIDDL IEAILLQAEV MEIKVSAEGP ARGVVIESRL DKGRGPVATI
LVQSGTLRKG DILLSGVETG RVRAMLTERG QEIIEAGPST PVEILGLSGT PNAGDEAVVV
PDERRAREIA GHRQAKEREV KLARQQSAKL ENMFNEMEEG EIRALNLVIK ADVQGSAEAL
SDSLTKLSTD KARVKVVAAG VGGINETDVN LAVASNAVII GFNVRADAAA RRLIAEKGID
LHYYSVIYNA IDEIKGALIG ILDPEYREEI IGLARVDDVF RSPKLGAIAG CLVIEGSVRR
NNPIRVLRDN IVVFEGQLES LRRFKDDVQE VRAGTECGIG VKDYKDVKVG DQIEVYERVR
KEPAL
