ID C9P1A5_VIBME Unreviewed; 900 AA.
AC C9P1A5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=VIB_000252 {ECO:0000313|EMBL:EEX38307.1};
OS Vibrio metschnikovii CIP 69.14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX38307.1, ECO:0000313|Proteomes:UP000005604};
RN [1] {ECO:0000313|EMBL:EEX38307.1, ECO:0000313|Proteomes:UP000005604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX38307.1,
RC ECO:0000313|Proteomes:UP000005604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA Vonstein V.;
RL Submitted (OCT-2009) 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 ECO:0000256|RuleBase:RU000645}.
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}.
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DR EMBL; ACZO01000004; EEX38307.1; -; Genomic_DNA.
DR RefSeq; WP_004394157.1; NZ_ACZO01000004.1.
DR AlphaFoldDB; C9P1A5; -.
DR STRING; 675813.VIB_000252; -.
DR GeneID; 79888551; -.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000005604; 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; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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; IPR009061; DNA-bd_dom_put_sf.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 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|ARBA:ARBA00022490, 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:UP000005604}.
FT DOMAIN 399..568
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 29..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..550
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 32..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 454..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 508..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 900 AA; 99261 MW; 4FC657FACE118E42 CRC64;
MTQLTVKALS EEIGTPVDRL LEQLADAGME KAGSDHVSEE EKQKLLTHLR KEHGEGSEPT
RLTLQRKTRS TLSVNAGGGK SKNVQVEVRK KRTYVKRSVI EDDAKREAEE AAQREAEEKA
KREAEAALKR EAEEKAAREA QEKAQREAEE KAKREAEEAQ RDVPVEVNQA KRERSAQDKS
KQEAARKEAE QLKRRQEEEA QRKIEEESQR QLEIARELAE KNKDRWSAEE EKKGNMQEDT
DYHLTTSTHA REAEDEADRR EEGARRAAKL KKTKLSSRDD KQERGSRTRG GKAGRKGRIN
KPTSMQHGFD KSAVVAKSDV VIGETIVISE LANKMSVKAT EVIKVMMKMG AMATINQVID
QETAQLVAEE MGHKVILRKE NELEEAILSD RDNKFELVSR APVVTIMGHV DHGKTSTLDY
IRRTHVADAE AGGITQHIGA YHVETPNGMI TFLDTPGHAA FTSMRARGAQ ATDIVVLVVA
ADDGVMPQTV EAIQHAKAAG VPLIVAVNKI DKEAANPDNV KNELAQYDIM PEEWGGENMF
VHISAKQGTN IDGLLEAILL QAEVLELKAV KEGMASGVVI ESRLDKGRGP VATVLVQSGT
LNKGDIVLCG QEYGRVRAMR DEVGNEIEHA GPSIPVEILG LSGVPSAGDE ATVVRDERKA
REVANYRQGK FRDVKLARQQ KSKLENMFSN MAAGDVAELN VVLKADVQGS VEAIAESLKK
LSTDEVKVNI VGSGVGGITE TDAVLAAASN AIVVGFNVRA DASARRTIED ENIDLRYYSI
IYQLIDEVKQ AMSGMLAPEF KQEIIGLAQV RDVFKSPKLG AIAGCMVTEG TIKRNSPIRV
LRDNVVIYEG ELESLRRFKD DVAEVKNGYE CGIGVKNYND VRVGDQIEVF EIVEIQRTID
//