ID A0A095XSQ6_9GAMM Unreviewed; 860 AA.
AC A0A095XSQ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HRUBRA_02674 {ECO:0000313|EMBL:KGE02696.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE02696.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE02696.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE02696.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(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: 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:KGE02696.1}.
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DR EMBL; AUVB01000085; KGE02696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095XSQ6; -.
DR STRING; 1265313.HRUBRA_02674; -.
DR PATRIC; fig|1265313.6.peg.2633; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_6; -.
DR Proteomes; UP000029640; 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; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029640}.
FT DOMAIN 360..529
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 73..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..511
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 140..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369..376
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 415..419
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 469..472
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 860 AA; 93377 MW; FFA6520F187ACBD3 CRC64;
MRDAGLPHKD AAEPVSDEDK QTLLTYLKQS HGESTAAPKR ITLKRKTMST LRTGGSSGKK
TVNVEVRKKR TYVKREESEA PAEEELAVTA ASADAELPET VPDEAPVVEA APVEEAPAPK
KEPEFEPLPE EEEEPEDLAN LDPEVLRQRA ALRRKQKEEE EAAARAAAIA ARQAEEEQRK
AAEAAAKARE EAPKRPKRLH AAPAEQPPRD DQKRKTRGRL SRNDSLGRGK QRGHNLSLSD
LDAAEGRTRR RGGRKKMKAT HEEHGRHGFE MPTERKVYEV EIADMISVGG LAEGMAVKSG
VVIKELMKLG VMATINQMID RDTATLVVEE LGHVAKYISA DALEEDLTET LAQHGGTPEP
RAPVVTVMGH VDHGKTSLLD YIRKAKVASG EAGGITQHIG AYHVETGHGM ISFLDTPGHA
AFTAMRARGA KSTDIVILVV AADDGVMPQT IEAVQHARAA EVPLIVAVNK IDKEGADPDR
VKNELSAQQV IPEEWGGDTQ FVHVSAITGD GIETLLDAVL LQADLLELKA PRDVPAQGIV
IESRLDKGRG PVASLLVQSG TLRQGEIVLA GLQYGRVRAM LDENGKPVDT AGPSIPVEIL
GLDGTPDAGD QFAVVENEKQ ARDLADYRQA KMRENKLQRQ QAAKLDNMFE SMTAGERKTL
NVVVKADVRG SLEAIQAALL ELGNDEVQVN IVTGGVGGIA ETDVTLAMTS GAVIFGFNVR
ADAAARQLVE SEGVDLRYYN VIYDLIDDVK QALSGMLAPE MREEIVGIAE VREVFNSPKL
GQIAGCMVTE GTVYRSKPIR VLRDNVVIYQ GELESLRRFK DDANEVRNGV ECGIGVKNYN
DVQVGDQIEV YEVKEVARSL
//
