ID M2YE26_9MICC Unreviewed; 971 AA.
AC M2YE26;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=C884_02412 {ECO:0000313|EMBL:EME36805.1};
OS Kocuria palustris PEL.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME36805.1, ECO:0000313|Proteomes:UP000009877};
RN [1] {ECO:0000313|EMBL:EME36805.1, ECO:0000313|Proteomes:UP000009877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEL {ECO:0000313|EMBL:EME36805.1,
RC ECO:0000313|Proteomes:UP000009877};
RX PubMed=24504000;
RA Sharma G., Khatri I., Subramanian S.;
RT "Draft Genome Sequence of Kocuria palustris PEL.";
RL Genome Announc. 2:e01261-13(2014).
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:EME36805.1}.
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DR EMBL; ANHZ02000008; EME36805.1; -; Genomic_DNA.
DR RefSeq; WP_006214467.1; NZ_ANHZ02000008.1.
DR AlphaFoldDB; M2YE26; -.
DR STRING; 71999.KPaMU14_08130; -.
DR Proteomes; UP000009877; 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; 1.10.10.2480; -; 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; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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:UP000009877}.
FT DOMAIN 463..635
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 32..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 522..526
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 576..579
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 971 AA; 101281 MW; 4F0DAA3E2CDE5C7B CRC64;
MAKQRVHELA KELGMTSKEA ISALQELGEF VRGASSTVEP PVAKKLKESP QAKAALAKKG
EKEGSAKAET SNPAAKPSLA GAKPAGGAKP GASSAPKPGQ SVPTPATAGQ TAQPEQKTEE
QAKPAEQAPP APAAESEPAA AQPEKPAAEK PSAEQAPAPE APSKPAPKPG SAAPKPGGPR
PGNNPFTPKQ AGGAQRPARS QGGPRPGNNP FAAQQGMGTQ RPGQAAQGGP RPGAPRPGQG
GPRPGAPRPG APRPGQGAGA GGPRPGGPRP SPNMMPGHTS NVAPVGTRPA RGGGAGGGRR
GGPGGPGGGP GGGFRPGGGP GRGGRGATQG AFGRGGPSRK GRKSKRAKRQ ELEQMNAPKV
GGVSVPHGDG NTVVRLRRGA SLMDFAEKID ANPASLVTVL IHLGEMATQT QSLDEETFEA
LGAELGYVIQ IVSPEDEERE LFESFDIDLE AEQAAEGEEQ LEKRPPVVTV MGHVDHGKTR
LLDAIRNTRV IEGEAGGITQ HIGAYQVSQE VDGEDRALTF IDTPGHEAFT AMRARGAQVT
DIALLVVAAD DGVMPQTVEA LNHAQAANVP IVVAVNKIDK PEANPEKIRG QLAEYGLVPE
EYGGDTMFVD VSARQSQNID ELLESIVLTA DGALELQANP NKDARGVAIE ANLDKGRGAV
CTVLVQSGTL RVGDSIVAGG AHGRVRAMFD ETGAAVEEAG PSRPVQVLGL STVPRAGDTF
IATEDERTAR QIAEKRQAAD RNALLAKRRK RVTLESFDQV VAEGKIDTLN LIIKGDVSGA
VEALEDSLLK IEVAPDEVQL RVIHRGVGAI TQNDVNLATV DNAVIIGFNV RPAERVTELA
DREGVEMKFY SVIYNAIDDV EAALKGMLKP EYEEVDLGKA EVREVFKSSK WGSIAGSYVT
EGLIRRNAKA RLVRDGNVVK EGLTIESLRR FKDDATEVRE GYECGIGLGS FNDIKEGDVI
ETWEMQEKPR A
//
