ID G5H5Z1_9BACT Unreviewed; 990 AA.
AC G5H5Z1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=HMPREF9450_00351 {ECO:0000313|EMBL:EHB93085.1};
OS Alistipes indistinctus YIT 12060.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB93085.1, ECO:0000313|Proteomes:UP000006008};
RN [1] {ECO:0000313|EMBL:EHB93085.1, ECO:0000313|Proteomes:UP000006008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB93085.1,
RC ECO:0000313|Proteomes:UP000006008};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alistipes indistinctus YIT 12060.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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:EHB93085.1}.
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DR EMBL; ADLD01000004; EHB93085.1; -; Genomic_DNA.
DR RefSeq; WP_009133157.1; NZ_JH370371.1.
DR AlphaFoldDB; G5H5Z1; -.
DR STRING; 742725.HMPREF9450_00351; -.
DR GeneID; 78317985; -.
DR PATRIC; fig|742725.3.peg.398; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_2_10; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000006008; 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; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000006008}.
FT DOMAIN 491..660
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 125..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..642
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 239..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 500..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 546..550
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 600..603
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 990 AA; 106434 MW; 01166752A7724A7C CRC64;
MPNVRRLRLH QVARELKVGQ TTIVEYLEKK GIKVENAPST LIEPHVYEVL DKEFGANKAE
TVNIREKINQ KLEAVSLGNR KDGAPAEDDA DFKKEVIIKS GVISVKDEVA AMSTPKILGK
IDLSGKKPAA APAEAKKPEL PSEKSVPAVA PAAEQKPAPA PAVKSEPVSQ PAAAAPKAPA
ATSVAPSAAA PVSTAAPEAT AAAPAAKAAP KAVAPAPASK PAAVAKPAAQ PVPVVSTRTA
DAAAQTQTYD ERVAADQTNL FRPNSEENRL SGPKVLGKID VNLLEKKGDF GRREKRKRIT
KDKVDLNQKP APGAPRTDGR SAAGGPGSGG GSGRGSFRDN NKKRGPKGAP KPAPVHTEVS
EEEVQKQIKD TLARLTSKGS KFKTAKHRRD KRDAVSARIQ EEQAREEREK SILKVTEFVT
VSELASMMDV GVTDVITACM NLGLMVSINQ RLDAEALVVV AEEFGYKIEF VTVDTQEAID
TEEDKPEDLV PRPPIVTVMG HVDHGKTSLL DNIRKTNVIA GEAGGITQHI GAYSVNVNGR
RITFLDTPGH EAFTAMRARG AQVTDVAIII VAADDSVMPQ TVEAINHAAA AQVPMVFAIN
KIDKPGANTD KIREELSAMN YLVEDWGGKY QSQEISAKKG INLDKLLEKV LLEAEMLDLK
ANPNRMAQGV VIESTLDKGR GYVATVLVQN GTLRVGDVML SGTYSGRVKA MFNERGTRIT
EAPPSTPVLV LGLNGAPQAG DTFNVMDDER SARDIANKRE QLQRMQGLRT QKHITLDEIG
RRIAIGNFKE LNIIIKGDVD GSIEALADSL IKLSKEEVQV NVIHKAVGPI SESDVLLAAA
SNAVIVGFQV RPSTSARRLA EKEEIEIRLY SIIYDAINDI KDAIEGMLAP VMKEEIVCSV
EVLETFKITK VGTVAGCIVR EGKITRNTPI RVIRDGIVVY TGKLGSLKRF KDDVKEVGPN
LECGLNIDNY NDIKVGDIIE GYEQVEVARK
//
