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Database: UniProt
Entry: A0A0F3L5N8_9CAUL
LinkDB: A0A0F3L5N8_9CAUL
Original site: A0A0F3L5N8_9CAUL 
ID   A0A0F3L5N8_9CAUL        Unreviewed;      1006 AA.
AC   A0A0F3L5N8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=VH88_14180 {ECO:0000313|EMBL:KJV38691.1};
OS   Brevundimonas sp. KM4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1628191 {ECO:0000313|EMBL:KJV38691.1, ECO:0000313|Proteomes:UP000033583};
RN   [1] {ECO:0000313|EMBL:KJV38691.1, ECO:0000313|Proteomes:UP000033583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM4 {ECO:0000313|EMBL:KJV38691.1,
RC   ECO:0000313|Proteomes:UP000033583};
RA   Sulaiman J., Priya K., Chan K.-G.;
RT   "Draft genome sequence of Brevundimonas sp. KM4.";
RL   Submitted (MAR-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJV38691.1}.
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DR   EMBL; JZRG01000032; KJV38691.1; -; Genomic_DNA.
DR   RefSeq; WP_045811819.1; NZ_JZRG01000032.1.
DR   AlphaFoldDB; A0A0F3L5N8; -.
DR   PATRIC; fig|1628191.3.peg.1711; -.
DR   Proteomes; UP000033583; 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}.
FT   DOMAIN          503..673
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..214
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..417
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         512..519
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         559..563
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         613..616
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1006 AA;  105675 MW;  0C7CF0835026C1C6 CRC64;
     MSDENDKTNQ GQGNTGGTPS QTGPRAPLSL KPRVVGSVPT GTVKQSFSHG RSKTVVVETK
     RRAGAGGPQR PQGFDVARPQ QAAQAPRPQG PRPSQPAGGA LSAEEQEARR RAIALATQAN
     AAKAAAEAAA KAAADAAARE QAAATERAAQ AARDEAAAAK AAAEAARAEA AKLTAAAPAA
     PAKPAPKPAA PVAAAPTPAP AAPAPAPAPA RPAAPARPVV NFGQRVPKPG NPQRAAPERP
     AFGGRSAREQ AMGGGDRAYS DRPQSDRPQG DRPQGARSGP GGQRPQGAKP AEPVRYSALN
     PRPAPGAARP GGPRTGPGGR AAPNAPPAEA NVLRPARAPG AGFGRPAGRD DDREKRFSDA
     GKAVSRTRGE PKRREGRMTI QSVVGDGDAA ERMRSLASVR RAREREKEKR KGGSTDAPNR
     PREVVIPDVI TVQELSNRMA VRGVDIIKFL MKQGLMMKIN DVIDSDTAEL VAEEFGMAVK
     RVSESDIETG FLGEADDADA SDTRAPVVAI MGHVDHGKTS LLDALRTTDV AGGEAGGITQ
     HIGAYQVRLP DDQKVTFLDT PGHAAFSAMR ARGANVTDIV VLVVAADDGV MPQTIEAIQH
     AKAANAPLIV AVNKMDKPGA TSQKVVNELL QYEVIAESLG GDTQIIEVSA KERMNLDGLL
     EAILIQAEVM DLRANADRSA EGVVIEAKLD KGRGPVGTVL VKRGTLKRGD IVVAGGSWGK
     VRALLNERNE QLTEAGPSVP VEILGLDEAP SPGDVFAVVD SEARARELTE YRQRVKREKA
     QVSGGSVSLV DMMAKLGSKK ISELPVVIKA DVQGSGEAIS ASLEKMGNDE VRARIVYSGA
     GGITESDVNL AKSAGAPILG FNVRASKQAR DLAEREGVEI RYYSIIYDLL DDMKGVLSGM
     LAPLQRETFL GNAQVLQVFD ISKIGKIAGC RVTEGVVRKG ARVRIIRDDV VVLELGVLNT
     LKRFKDEVNE VPSGQECGMQ FQGFQDIKEG DYIECFTVEE IKRTLD
//
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