IF2_AGRFC
ID IF2_AGRFC Reviewed; 913 AA.
AC Q8UJ51;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Atu0087;
GN ORFNames=AGR_C_131;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007869; AAK85907.1; -; Genomic_DNA.
DR PIR; AB2587; AB2587.
DR PIR; B97369; B97369.
DR RefSeq; NP_353122.1; NC_003062.2.
DR RefSeq; WP_010970645.1; NC_003062.2.
DR AlphaFoldDB; Q8UJ51; -.
DR SMR; Q8UJ51; -.
DR STRING; 176299.Atu0087; -.
DR EnsemblBacteria; AAK85907; AAK85907; Atu0087.
DR KEGG; atu:Atu0087; -.
DR PATRIC; fig|176299.10.peg.80; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q8UJ51; -.
DR BioCyc; AGRO:ATU0087-MON; -.
DR Proteomes; UP000000813; Chromosome circular.
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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 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..913
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137164"
FT DOMAIN 411..578
FT /note="tr-type G"
FT REGION 1..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..427
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 445..449
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 466..469
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 520..523
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 556..558
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 42..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 420..427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 466..470
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 520..523
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 913 AA; 98822 MW; 2BF1CEE264C484D8 CRC64;
MTDNNDDKTL NAPAKKTLTL KPGGMNQGTV RQDMGRGRTN AVVVETRKRR PHRPEDEKPV
QPVVAAPKPA APAPVAARPQ APQPRIHQPG GQQQRPGSSQ SQQRSGSSAP QQRQADRPRG
NVLHDLSAGE MEARRRALME AQARDVVEAK QRAEDEARRK VEEEQRIAAE KMEAANRAAE
EAAAAKVAAS QPAAEVRAEP ASERPAAAAA PAPRTDARPQ SAAAAPRSAP ATPDAAAPRG
RRTGGDDEDD RGAVRRGSSL PARGKVVAPA PAKPAARLKT EEERRRGKLT VTSNLEEDGT
PRGRSMASMR RRQEKFRRSQ MQETREKVLR EVILPETITI QELSQRMSER AVDVIKFLMK
EGQMLKPGDV IDADLAELIA VEFGHTVKRV SESDVEEGIF NQTDDEGEMV SRPPVVTIMG
HVDHGKTSLL DAIRQANVVS GEAGGITQHI GAYQVEKNGH KITFIDTPGH AAFTAMRARG
AQATDIAVLV VAADDSVMPQ TIESINHAKA AGVPIVVAIN KIDKHEANPD KVRQQLLQHE
VFVESMGGEV LDVEVSAKNK LNLDKLLEAI LLQAEILDLK ADPSRTAEGT VIEAELDRGR
GAVATVLVQK GTLKPGQIIV AGDQWGRVRA LVNDKGDHVK EAGPAMPVEI LGLSGTPSAG
DRFAVVENES RAREISEYRQ RLARDKAVAR QTGQRGSLEQ MMSQLQTSGL KEFPLVIKAD
VQGSVEAIIA SLDKLGTDEV RARVVHSGAG AITESDISLA EASNAAIIGF NVRANAQART
ASERAGIEIR YYNIIYDLVD DVKAAMSGLL SPERRETFLG NAEILEVFNI TKVGKVAGCR
VVEGKVERGA GVRLVRDNVV IHEGKLKTLK RFKDEVNEVP VGQECGMAFE NYEDIRAGDT
IECFRVEHIT RTL