ID A0A0K0Y9P7_9RHOB Unreviewed; 825 AA.
AC A0A0K0Y9P7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ECO:0000313|EMBL:AKS47678.1};
GN ORFNames=OSB_31650 {ECO:0000313|EMBL:AKS47678.1}, SAMN05444287_2665
GN {ECO:0000313|EMBL:SIO39935.1};
OS Octadecabacter temperatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS47678.1, ECO:0000313|Proteomes:UP000067444};
RN [1] {ECO:0000313|EMBL:AKS47678.1, ECO:0000313|Proteomes:UP000067444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB1 {ECO:0000313|EMBL:AKS47678.1,
RC ECO:0000313|Proteomes:UP000067444};
RX PubMed=26358607;
RA Voget S., Billerbeck S., Simon M., Daniel R.;
RT "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT Mesophilic Species of the Genus Octadecabacter.";
RL Genome Announc. 3:e01051-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000184809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26878 {ECO:0000313|Proteomes:UP000184809};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SIO39935.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 26878 {ECO:0000313|EMBL:SIO39935.1};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP012160; AKS47678.1; -; Genomic_DNA.
DR EMBL; FSRP01000002; SIO39935.1; -; Genomic_DNA.
DR RefSeq; WP_049835846.1; NZ_FSRP01000002.1.
DR AlphaFoldDB; A0A0K0Y9P7; -.
DR STRING; 1458307.OSB_31650; -.
DR KEGG; otm:OSB_31650; -.
DR PATRIC; fig|1458307.3.peg.3188; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000067444; Chromosome.
DR Proteomes; UP000184809; 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; 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; 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 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; PF08364; IF2_assoc; 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:UP000067444}.
FT DOMAIN 323..493
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 379..383
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 433..436
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 825 AA; 88491 MW; 1A5EBE1C9F9454A5 CRC64;
MSDSDGKKPL GVTPRPGSVK QSFSHGRTKN VVVETKRKRV VVPKPGAAKP TGSSAPLGGD
PSKRPAGISD VEMDRRMKAL QAAKAREAED AAKREADEKA RAAERERRLA EIAEKERADK
ERDEAVKAKQ DEEERKKRDA EAAAQAAAAP AAVDPELAPA QRRAPPSGGA PAATPRKKED
DRDSRKNKNQ GDARKGGKLT LNQALRGGEG GRHRSMAQMK RKQDRARQKA MGQSVEREKV
MRDVQLPEAI VVSELANRMS EKVSDVVKAL MTNGIMATQN QTIDADTAEL IVEEFGHKVV
RVSDADVEDV INIIEDDEKD LKGRPPVITI MGHVDHGKTS LLDAIRNAKV VAGEAGGITQ
HIGAYQVTTD NGAVLSFLDT PGHAAFTSMR ARGAQVTDIV VLVVAADDAV MPQTIEAIAH
AKAANVPMIV AINKCDRPAA NPDKVRTDLL QHEVIVEKMS GEVQDVEVSA ITGQGLDELL
EAIALQSELL ELKANPDRAA QGAVIEAQLD VGRGPVATVL VETGTLRRGD IFVVGEQWGK
VRALIDDKGE RVNEAGPSVP VEVLGLNGTP EAGDVLNVTE TEAQAREIAE YRANAAKEKR
AAAGAAVTLD QLMANAKADE NVSELPILVK GDVQGSTEAI VQAMAKIGND EVRVRVLHSG
VGAITESDIG LAEASGAPVI GFNVRANASA RNSANQKGVE IRYYSIIYDL VDDVKAAASG
LLSAEVRENF IGYAKIQEVF KVSNVGKIAG CLVTEGVARR SAGVRLLRDD VVIHEGTLKT
LKRFKDEVKE VQSGQECGMA FENYEDIRAD DVIEIFEREE VERNL
//
