ID A0A0S8AF33_9BACT Unreviewed; 782 AA.
AC A0A0S8AF33;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=AMK71_12185 {ECO:0000313|EMBL:KPJ97976.1};
OS Nitrospira bacterium SG8_35_4.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704025 {ECO:0000313|EMBL:KPJ97976.1, ECO:0000313|Proteomes:UP000050997};
RN [1] {ECO:0000313|EMBL:KPJ97976.1, ECO:0000313|Proteomes:UP000050997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_4 {ECO:0000313|EMBL:KPJ97976.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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: 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:KPJ97976.1}.
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DR EMBL; LJTM01000255; KPJ97976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8AF33; -.
DR PATRIC; fig|1704025.3.peg.1646; -.
DR Proteomes; UP000050997; 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 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 280..449
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 47..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..431
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 77..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 335..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 389..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 782 AA; 86125 MW; 8B9C3DB5011559C8 CRC64;
MRIYELSKNI NVSSKEIIAK LAGLGIAVKS HMSNIDEETA KKLSDIFSTG KPSRVKEKAP
SGTSKGKALK SAPVKTDALK KTQESKAKPE KKAVPEGKNK ALKKPPIRQA EEISDKEEPS
IEEDEVIVPD RFRKEIDTEK LTKMKVKPGM QRAFDSIRRV EVNKKGPDFR PRFKKHDKKQ
PLKKAEPVEA PSATAPRKRI LKFQEGSTVK EFSELIGQKL NDVMKKFMEL GYMLTINQPL
DADAAQIVAE SFGIKIELTS IEDEEAFLEQ EEVDEKALSP RPPIVTIMGH VDHGKTTLLD
AIRETKVTET EAGGITQHIG AYKVKLKGKE IAFLDTPGHE AFTMMRARGA KVTDIVILVV
AADDSVMPQT IEAIDHAKAA NVPIVVAVNK IDKPEANIDK VKTELSQRDV TPEDWGGKNI
FVEVSAKQKT GLDHLLEMVL LQAEMMELKA DYTRPARGTV VEAKLDRGRG PVGTVLINSG
ILKTGDAFLV GTIAGKVRAL IDDNGKKIDQ AGPSTPVEVI GFPEVPHAGD IFAVMEDERK
ARQIAMNRLQ KQRTAAIVRK KKLTLDDLYQ RVKEGEIRDL NVIIKADVQG SVEAVKDALS
SISHPEVKVN VIHTGAGGIN ESDVMLAAAS NAIIIGFNIR PDANATPLIE KEGIDVRLYT
VIYEAIEDIK KALEGLLEPT ITEKVIGRAE VRNLFQVSRL GVIAGCYVVE GKMSRASAGV
RVIRDNIVIY ESRISSLKRF KDDAKEVQTG FECGIMIENF NDLKVGDIIE NYVREEVAAK
LE
//
