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Database: UniProt
Entry: Q0EZ74_9PROT
LinkDB: Q0EZ74_9PROT
Original site: Q0EZ74_9PROT 
ID   Q0EZ74_9PROT            Unreviewed;      1045 AA.
AC   Q0EZ74;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=SPV1_07641 {ECO:0000313|EMBL:EAU54550.1};
OS   Mariprofundus ferrooxydans PV-1.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU54550.1, ECO:0000313|Proteomes:UP000005297};
RN   [1] {ECO:0000313|EMBL:EAU54550.1, ECO:0000313|Proteomes:UP000005297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV-1 {ECO:0000313|EMBL:EAU54550.1,
RC   ECO:0000313|Proteomes:UP000005297};
RA   Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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: 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:EAU54550.1}.
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DR   EMBL; AATS01000007; EAU54550.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0EZ74; -.
DR   STRING; 314344.AL013_00355; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   InParanoid; Q0EZ74; -.
DR   OrthoDB; 5287317at2; -.
DR   Proteomes; UP000005297; 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; 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:UP000005297}.
FT   DOMAIN          545..713
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          55..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         554..561
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         601..605
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         655..658
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1045 AA;  110843 MW;  8A89189F6D0A6090 CRC64;
     MAKRILDLAK ELGVDAAEIQ RVAVQCNVVV SGPTSTLDTD DLKKIRASLQ SKVEAAPAKT
     GGKTLTLNRP MVAGQPRSGG RVEGRGRSVE VSVRRRHTPV KAQPTVAEQT PQADAVETPA
     AAAPKAKPLA PAQRAAAAVE QRKLTEAANK AAAEQQKAAD AKAAASEPAA AEAPKVPASK
     PEVAAQPAVS RETATKSPVT RQPIKRQAGV ASKPTDTPGV VRRSAVNPAE VARSKIAAAA
     AARTAAQEKS NQERVARQRA AQTRNTPAGT GGAAAQGRPG QVGAPARTRQ APGGPNRSPQ
     DRRPAQGAQS PGHKGPRTTI RRGLTPAQIA ASKAPSSSLK QIEQKISEER ATRRKTQQRP
     ASGARPGGAA NQGMTRRTPS VAISPSADAP AAPTGPQRRR GAPGAQRGQR RLSPAEKAAR
     RDYASKRNVV LTPQQEERMA RLARGSKRRN QITKDDENFV VRTVEVTDPI MIQELASRMA
     IKSAEVVKKL FEMGSMVTVN EGIDGETAVL IVEEFGHKAK IINAGAVEDV LIEDVSEDDD
     TDLQPRPPVV VVMGHVDHGK TSILDALRKA HVAAGEAGGI TQHIGAYMVK LASGERVVFI
     DTPGHEAFTS LRARGAGMTD VAVLVVAADD GVMPQTIEAL NHAKAAGVPM IVAVNKMDKE
     GADPEKVMRQ LADHGVLSED WGGDTIFVPV SAHTGLGLDE LLDMLALQTE ILELNANPKR
     RGKGIVIESR LDRGRGPVAT VLVQNGTFKQ GDTVVVGSVT GRIRAIVDEN AKQHRTAGPS
     IPFELLGLDS VPESGQEIFT VESEKQARDI VRYRKDKERE QGAEAMKRAS MDELFANLQS
     GMKEVPVVIK GDVTGSVDAM ADSLAKAGTD EVKVKVVHKG IGGITESDVM LASASNAIVI
     GFNVRPEAKA KRLAEQEGID VRFYKIIYDA IDDMKAAMAG VLSPDKVEKV TGSADVREVF
     QAPKIGAIAG CYVTDGYVTR GSNVRVLRDG VVVYDGVLAS LRRFRDDVKE VKTGFECGIG
     VEKFNDIKEG DSFEFYIIEE VAATL
//
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