ID A0A1M4TA95_9BACT Unreviewed; 989 AA.
AC A0A1M4TA95;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SAMN05443144_101246 {ECO:0000313|EMBL:SHE41288.1};
OS Fodinibius roseus.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHE41288.1, ECO:0000313|Proteomes:UP000184041};
RN [1] {ECO:0000313|EMBL:SHE41288.1, ECO:0000313|Proteomes:UP000184041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21986 {ECO:0000313|EMBL:SHE41288.1,
RC ECO:0000313|Proteomes:UP000184041};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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; FQUS01000001; SHE41288.1; -; Genomic_DNA.
DR RefSeq; WP_073058983.1; NZ_FQUS01000001.1.
DR AlphaFoldDB; A0A1M4TA95; -.
DR STRING; 1194090.SAMN05443144_101246; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000184041; 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}.
FT DOMAIN 481..651
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 56..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..134
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490..497
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 537..541
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 591..594
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 989 AA; 109584 MW; B4E3FAA3D248F0C5 CRC64;
MSPKDRPKRL FKVASEFNVS TTSIVGSLSD EGFEVANKPN TKITPEMYEV LEEVYGTDKA
NSQQHAKAKE EYASRRDQIR SSRNESISIE DTLEPLEDEL PLEPEEDDEP EEIAGLTPIE
EEEGESEDAP EEAAASAGEE EKEISGEAEP EEEPPAEEES EGPEPVEAEE QPEDAEEAED
EAYEADEEVP EEVTASAGDE EKEISGETEP EEEEPPAEEE SEEPEPVEAE EQPEDTEEAE
DEAYEADEEV PEEVTASAGE DEEGVEDEYD EEEEESEEEG VIRGRAGRLK GTKVVGKVKI
DESKPKRRKK RKRKKDRLGD DSSSTKKKSK KQDKKKKKKS RRRGKRVDEE DVEQKMKETL
RKMQSSETVG SRRQKRRRQR KEEREEEEQL QAELEELEEQ ILEVTEFITV SDLADLMGVK
ANEVITTCMN LGMMVSINQR LDASTIELVA EEFGYEVEFV DAEEAIEEIQ LEEDDPEDLE
PRAPIITVMG HVDHGKTSLL DYIRKSHVAE GEAGGITQHV GAYEVQTDDD RPITFLDTPG
HEAFTAMRSR GAKATDIVIL VVAADDAVMP QTIEAINHAK AGGVPIIVAI NKMDKPGADP
DKIKQQLAEY DVIVEEYGGT NQAAEVSAMT GDGIPELLDK VLIEAELMEL KANPDRTADG
VVLEARVDKG KGIVANILVQ NGTLEVGDAF VAGPCFGRVR AMENEHGNRV ESAGPSVPVQ
LTGFDDIPQA GDKLVVLEDE KKAKDIANQR QQIRREQELR KSKHLTLDDL SRRLALGEVS
DLNIIIKADV DGSIEALSGS LQKLSNEEVS VNIIHTAAGA ITESDVLLAS ASDAIIIGFQ
VRPTTNARAV AEEEEIDIRL FSVIYDAVDE VKDAMEGMLS PEISEKLYGN AEVREIFKVS
NVGTIAGCYV TDGKINRNNP VRVVREGVVI YDGEIDALKR FKDDVKEVQT GYECGISIVN
YNDIKVGDVI ENYEIVEERR SLEDVQDNS
//
