ID A0A098R1G8_9SPIO Unreviewed; 861 AA.
AC A0A098R1G8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=DC28_02030 {ECO:0000313|EMBL:KGE73975.1};
OS Spirochaeta lutea.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73975.1, ECO:0000313|Proteomes:UP000029692};
RN [1] {ECO:0000313|EMBL:KGE73975.1, ECO:0000313|Proteomes:UP000029692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC230 {ECO:0000313|EMBL:KGE73975.1,
RC ECO:0000313|Proteomes:UP000029692};
RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT "De novo Genome Sequence of Spirocheata sp.";
RL Submitted (MAY-2014) 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: 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:KGE73975.1}.
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DR EMBL; JNUP01000001; KGE73975.1; -; Genomic_DNA.
DR RefSeq; WP_037544487.1; NZ_JNUP01000001.1.
DR AlphaFoldDB; A0A098R1G8; -.
DR STRING; 1480694.DC28_02030; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000029692; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029692}.
FT DOMAIN 345..514
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..496
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 1..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354..361
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 400..404
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 454..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 861 AA; 94141 MW; AC7D9D9DC5947653 CRC64;
MSDDQNTEKS EQKPKATLIK HRKDDEATSP QDKTSSDSRK RVVKKKVVIK KKVHTDHEER
EGQAKPVKRD TEASQERGEE TKTPPKEAKS ASSQPSSGSQ TKPNPEKAPR KTTPDAKPGE
NRPRAAGPRQ AGNLARKQGN LAGRDTSSGK RSYPTKAGIV GGRYVGPDRN SGPGRGQQGG
PGGPGGDRNR PPRPPQRNFR PGGPGGRPGS TPPPPDAAPE EKKASSKKFF KAKKKDNFQK
RDRHQEKEIH FKSKKPKIKT NPVPKEVSIM EVITVSELAK KMNLKASDLI AKLMAMGMMV
TINQQIDADT AQILAAEYDC KVNIVSLYDE TLIESPKDTE ADLEHRPPIV TVMGHVDHGK
TKLLDAIRKT NVVNDEAGGI TQHIGAYQVE TSRGKVTFID TPGHEAFTLM RARGAQVTDI
VILVVAANDG VMPQTLEAIS HAKDAKVPII IAINKVDLPE ANIDRVKQQL ADRGLLTEDW
GGDVMSCPIS ALKGEGINEL LDAVLLQAEV MELKANYKGV AEGKVIESRI DQGRGTVSTV
LIERGCLKVG DSFVAGVYPG KVRAMFNDRG QKVDEAGPSM PVEILGFTGI PEAGVPFQVT
ESDRMARQVG EKRQELQKVE NAKNVKKITL DNLYDSIQQG EIQELKVIIK GDVHGSVEAI
QSALEKLSTQ EIHLVVVQAA AGAINERDIM LAAASNAIII GFHVRPTPKA QAFADQEKVE
IRKYSIIYDV VEDIRQAMEG MLSPELREEQ IGTVEVRETF KVPKQGVIAG SYVTNGEVRR
NAQVHLIRDG IEIFTGPIVS LRRFKDDAKE VKAGFECGIG LENWIDIQTG DTMEVFVMKE
VAKKLGPTLE EIKKSSEKKK K
//
