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Database: UniProt
Entry: C9P1A5_VIBME
LinkDB: C9P1A5_VIBME
Original site: C9P1A5_VIBME 
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
//
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