ID A0A0B6TGM1_9CORY Unreviewed; 966 AA.
AC A0A0B6TGM1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 02-APR-2025, 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 ECO:0000313|EMBL:AJK69127.1};
GN ORFNames=B840_07645 {ECO:0000313|EMBL:AJK69127.1};
OS Corynebacterium marinum DSM 44953.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK69127.1, ECO:0000313|Proteomes:UP000031928};
RN [1] {ECO:0000313|EMBL:AJK69127.1, ECO:0000313|Proteomes:UP000031928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK69127.1,
RC ECO:0000313|Proteomes:UP000031928};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium marinum DSM 44953.";
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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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}.
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DR EMBL; CP007790; AJK69127.1; -; Genomic_DNA.
DR RefSeq; WP_042621642.1; NZ_CP007790.1.
DR AlphaFoldDB; A0A0B6TGM1; -.
DR STRING; 1224162.B840_07645; -.
DR KEGG; cmq:B840_07645; -.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000031928; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 FunFam; 2.40.30.10:FF:000007; Translation initiation factor IF-2; 1.
DR FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 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; IPR053905; EF-G-like_DII.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd.
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; PF22042; EF-G_D2; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00173; RAS; 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.
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:UP000031928}.
FT DOMAIN 462..634
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 54..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..140
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..253
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..324
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..349
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 471..478
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 521..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 575..578
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 966 AA; 99372 MW; 2AE0B4C9946B56A0 CRC64;
MPGKLRVHEL AKQLGVTSKE LLATLKEQGE FVKTASSTVE PPVVRKMLDV YEKDTAPKPG
AASAKPGAAG KPGPKPGGAP KPGAATKPGP KPAPAAKPTP APAAAAKPTP AAAAKPAPAP
TPAAAAKPTP APTPAAAAKP APTPAAAPKP EADAPTPAAA AGKPGPKPGP AAKPAPKPGG
APKPGSAMPR PMPRPGGRPR VANNPFSSGG GDRPAPRPGG GRGQGAPRPG GAGAPGGRGG
QGAPRPGGQG GQGAPRPGSD RPAQGGGRRP SPGMMPTSQA PTPGQMPQKA AGAGRGRGGQ
GGPGGRTGGP GGGGGGGFRG GGPRRGSTAG AFGRPGGAPR RGRKSKRQKR SEYEAMQAPN
VVGGIRLPDG RGQSIRLRRG ASLSDFADKI NADPAALVQA LFNLGEMVTA TASVSEETLQ
LLGAEINYVV QVVSPEDEDR ELLESFDLQF GEDEGGEEDL AKRPPVVTVM GHVDHGKTRL
LDTIRKADVG AGEAGGITQG IGAYQIRRVV DGRERPITFL DTPGHEAFTA MRARGAKSTD
IAILVVAADD GVMPQTVEAI NHAKAAGVPV VVAVNKIDKP DASPEKIRGQ LTEYGLVPEE
YGGDTMFVDI SAKQGTNIDE LLEAVVLTAD ASLDLRANPD MYAQGVAIEA NLDRGRGPVA
TVLVQRGTLR VGDSIVVGGT YGRVRRMIDE HGHDVEEAGP SRPVQMQGLN GVPGAGDNLL
VVEDDRVARQ IAAQRDARKR SAAQARGRKR VSLEDLDAVL KETSVLNLIL KGDNAGSVEA
LEESLLKIEM NDEVELNIID RGVGAVTQTN VSLANASNAV IIAFNVRAEG KATEEANTEG
VDIRYYTVIY RAIEEVEAAL KGMLKPVYEE REVGVAEIRA LFKASAIGLI AGCMVESGKV
RRNASARLVR DGNVIANNVK IESLRREKDD VTEVTAGYEC GLVLSYPDIA VGDKIQVFEQ
VEVPRD
//
