ID K9VRD3_9CYAN Unreviewed; 1054 AA.
AC K9VRD3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=Osc7112_5562 {ECO:0000313|EMBL:AFZ09785.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ09785.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ09785.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ09785.1,
RC ECO:0000313|Proteomes:UP000010478};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) 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; CP003614; AFZ09785.1; -; Genomic_DNA.
DR RefSeq; WP_015178991.1; NC_019729.1.
DR AlphaFoldDB; K9VRD3; -.
DR STRING; 179408.Osc7112_5562; -.
DR KEGG; oni:Osc7112_5562; -.
DR PATRIC; fig|179408.3.peg.6938; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000010478; 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; 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 PRINTS; PR00315; ELONGATNFCT.
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:UP000010478}.
FT DOMAIN 549..721
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 51..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 558..565
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 608..612
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 662..665
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1054 AA; 112183 MW; 781A187615B06C19 CRC64;
MNNGKVRIYE LSRELNLDNK DILAVCERLN ISVKSHSSTI TESEAERIRK TAEKYVASSH
SSPGKPAPPE RAAAPSRESG PHPNDQQKKQ QILEIRSPKV RPAGASSQPA GNEEKKNQPA
ATVATPPKSP AAQQLQPPAK PNINRPVLSK PNVAVSAAPS EVSETVGAIA PETTAQAQAP
APPQPPSEKA PERTQQPPTA PPAPSAKLTS PPVRAASESP SRTPQNLGNK PVLKLAKTEQ
EQSGQSETLE APAKPSRPSR PAPGSATESR DAQRPRREGA GGPVKTQLAD RPQPGGPRRS
LAPATSATGL RSRGGDTGAV GDDTDDHEED NTPLLEIPLL SRPTLPRPAK KTSVIWEEDD
DENSDAAKAA KAVKAKRSRL KPIDEDDDEL ENGLDLPAPV TVSLSLARPA KAKGQAAPKS
TPTPGAPGSS GKNKRPSPSH DKSSSGSSGG RGNRGKTAEA KVERPEKLLL SRPMTVQELA
FSLAVPETEI IKRLFSKGIA VNITETLDIP AVRMVAEEMG VEVETPEKVA PAIKVIEMLD
AADLEYLERR PPVVTIMGHV DHGKTTLLDS IRKTKVAQGE AGGITQHIGA YHVDVEHEGK
SQQVVFLDTP GHEAFTAMRA RGTRVTDIAI LVVAADDGVR PQTIEAISHA KAAKVPIVVA
INKVDKEGAQ PERVKQELTE YGLVADDWGG DITMVPVSAI RGENLDTLLE MILTVAEMED
LNANPHRPAK GTVIEAHLDK ARGPVATLLV QNGTLRVGDI VVAGSALGKV RAMIDDRGDR
VDQATPSFAV EVLGLREVPR AGDEFDVFAN EKEAAAIASG RATSRRDSRL LQGGRISLSG
FSQQAKEGVL KELNLILKAD VQGSLEAIVG ALTQLPQKEV QLRLLLSAPG EITETDIDLA
AASNAVIIGF NTTLATDARL AADQAGVDVR EYSIIYNLLD DIQGAMEGLL EPELVEEPLG
QVEVRAVFAI GRGAVAGCMV LSGKVIRNCK VRVRRGNNVV YEGVLDSLKR MKEDAKEVNA
GFECGISLSG FSDWAEGDMI EAYRMVTKRR TLSQ
//
