ID I3C4P4_9FLAO Unreviewed; 981 AA.
AC I3C4P4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=JoomaDRAFT_1575 {ECO:0000313|EMBL:EIJ38587.1};
OS Galbibacter orientalis DSM 19592.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ38587.1, ECO:0000313|Proteomes:UP000004690};
RN [1] {ECO:0000313|EMBL:EIJ38587.1, ECO:0000313|Proteomes:UP000004690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ38587.1,
RC ECO:0000313|Proteomes:UP000004690};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Improved High-Quality Draft genome of Joostella marina DSM 19592.";
RL Submitted (FEB-2012) 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 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}.
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; JH651379; EIJ38587.1; -; Genomic_DNA.
DR RefSeq; WP_008611827.1; NZ_JH651379.1.
DR AlphaFoldDB; I3C4P4; -.
DR STRING; 926559.JoomaDRAFT_1575; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000004690; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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|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:UP000004690}.
FT DOMAIN 479..647
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 83..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 535..539
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 589..592
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 981 AA; 108754 MW; D8A8C90619A075F4 CRC64;
MAESAKLRLN KVLRELNISL DRAVEYLSSK GHEVEARPTA KITNEVYNVL LDEFQTDRSK
KVASKEVGEE KRKEKEAIRQ ELEKENELKR QKQEEHEVVK AKANLAGPKT VGKIDLDGKK
EQAAPEKPKE EVQAEKVETP QPEKQPEKPK EEVSKPAESK VEENKELDKK VEEPKAEVEK
PVEVKPTESK PEPKKETEPA KPKQEVPQQK PKQESKPEPK PVQKEPVVPK ETKKVIVDGE
EVDSEQVKTK YTKLSGPNFT GEKIDLSQFN KPKKKKEDPK AADKKGAKAA DDKKKRRRRI
SKDNNNKGPR PNTGGGNNAG GNRFSKDRNN ARGKGRRNTA PVEKVEPTEE EVQKQVRETL
EKLQGKSNKS KGAKYRREKR DFHRQKSEKE LAQQEAESKV LKVTEFVTVS EVATLMDVPV
TQIISACMSL GMMVTMNQRL DAETLSIIAD EFGYEVEFIT TDIEEDVEVV LDAPEDLIHR
APIVTVMGHV DHGKTSLLDY IREENVIAGE SGGITQHIGA YGVTLKDGQK IAFLDTPGHE
AFTAMRARGA QVTDLAIIVI AADDNVMPQT KEAISHAQAA GVPIVFAINK VDKPTANPDK
IKESLAQMNL LVEDWGGKIQ SQDISAKTGQ GVPELLEKVL LEAEILELKA NPNKIANGTV
VEAYLDKGRG YVSTVLVQAG TLKIGDYVLA GTHSGKVKAM QDERGNDIKV AGPSTPISIL
GLDGAPQAGD KFNVYEDERE AKQIATKRTQ LQREQSVRTQ RHITLDEIGR RIALGDFKEL
NIILKGDVDG SVEALTDSFQ KLSTEEIHIN IIHKAVGPIT ESDVLLASAS DAIIIGFNVR
PMGNARSVAD KEEIDIRTYS IIYDAINDLK DAMEGMLSPE LKEEITGTAE IRETFKISKV
GTIAGCMVTD GKVYRNSGIR LIRDGVVVYT GELTSLKRFK DDVKEVSKGY DCGLQIKNYN
DIQVGDVVES FREVEVKKKL K
//
