IF2_BARHE
ID IF2_BARHE Reviewed; 845 AA.
AC Q6G4W7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BH02150;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; BX897699; CAF27027.1; -; Genomic_DNA.
DR RefSeq; WP_011180166.1; NC_005956.1.
DR AlphaFoldDB; Q6G4W7; -.
DR SMR; Q6G4W7; -.
DR STRING; 283166.BH02150; -.
DR PaxDb; Q6G4W7; -.
DR PRIDE; Q6G4W7; -.
DR EnsemblBacteria; CAF27027; CAF27027; BH02150.
DR KEGG; bhe:BH02150; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000421; Chromosome.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43381; PTHR43381; 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; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..845
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228170"
FT DOMAIN 343..510
FT /note="tr-type G"
FT REGION 44..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..359
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 377..381
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 398..401
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 488..490
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 44..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 845 AA; 93649 MW; 0E37C2DC663B0675 CRC64;
MSENNNDKIT VKRTLTLKRS VLETSTVKQN FSHGRTKAVV VETKRRKITR TDEKAETPQP
ITKPHVAPQR SRPRFEDAKP NEPTAKSNLS SAEIEARLRA LEEAHIQERI IREQAEEEAR
RAKEREESLR QTIQKTEIDE TPQEEEEPTL QTQTPSLSPA QSQIEPINIP ITPKNTTVIE
KRKADETKED DRNSRRTNLA KSEVRAPKVL KGADEKRRGK ITLNSALDEE GSARGRSMAA
MRRRQEKFKR AQNQEPKEKI SREVILPETI TIQELAQRMT ERSVDVIKFL MKQGQMMKPG
DVIDADVAEL IAVEFGHTVK RVLESDVEEG IFNIADNPQK MQLRPPVVTI MGHVDHGKTS
LLDAIRKANV VSGEAGGITQ HIGAYQVEKN GQKITFIDTP GHAAFTAMRA RGARVTDIAV
LVVAADDSVM PQTIESINHA KAAGVPIIVA INKIDKPTAN AQKVRTELLH HEVFVETMGG
ETLEVEVSAK TGQNLDKLLE AILLQAEILD LKADPQRTAE GVVIEAKLDR GRGSVATVLV
QKGTLHPSDI IVAGNEWGRV RALIDDHGRH VKEAVPSTPI EILGMQGTPQ AGDRFAVVTH
EAKAREIAEY RQRLARDKAV ARQTGSRGSL EQMMSKLQTT GVKEFPLIIK GDVQGSIEAI
ASALEKLGNE EVRARIVHSA AGGITESDIS LAEASHSAVI GFNVRANKQA RDCAKTQGIE
IRYYNIIYDL VDDIKAAMSG LRSPEQRETF LGNAEILEVF NITKIGKVAG CLVTEGKIER
GAGVRLIRDN IVIHEGKLKT LKRFKDEVNE VQSGQECGIA FENYEDIRTG DIIETFHIEH
INRTL
