IF2_BARBK
ID IF2_BARBK Reviewed; 848 AA.
AC A1UU50;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=BARBAKC583_1254;
OS Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-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: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; CP000524; ABM45132.1; -; Genomic_DNA.
DR RefSeq; WP_005767983.1; NC_008783.1.
DR AlphaFoldDB; A1UU50; -.
DR SMR; A1UU50; -.
DR STRING; 360095.BARBAKC583_1254; -.
DR EnsemblBacteria; ABM45132; ABM45132; BARBAKC583_1254.
DR KEGG; bbk:BARBAKC583_1254; -.
DR PATRIC; fig|360095.6.peg.1230; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000643; 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; Reference proteome.
FT CHAIN 1..848
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008201"
FT DOMAIN 346..513
FT /note="tr-type G"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..362
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 380..384
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 401..404
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 455..458
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 491..493
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 401..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 455..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 848 AA; 93750 MW; 0BA453C00EC016CC CRC64;
MSENNNDKIT AKKTLTLKRS GSETNTVKQN FNHSRTKAVV VETKRRKIAR PDEKTEMPQP
ITKPHVAPPR SKPRIEKPVL VTPTAQSNLS STEMDARLRA LEEAHIQDEI IRKQAAEKQI
AERQAAEKQA KESEEGLHLQ KTHKEKIQKS SSNTTKPTPL FSSTVSPIES IEAALTLKNT
AASKRKADEN DDDEKYNRRA NLSKSEIRAP KIIKGTDERR RGKLTLNSAL DEEGNSRGRS
MAAMRRRQEK FKRAQNQEPR EKISREVILP ETITIQELAQ RMAERSVDVI KFLMKQEQMM
KPGDVIDADI AELIAIEFGH TVKRVSESDI EEGIFNVDDD PQKMKTRPPI VTIMGHVDHG
KTSLLDAIRK ANVVSSEAGG ITQHIGAYQV EQNGQKITFI DTPGHAAFTA MRARGAQITD
IAVLVVAADD SVMPQTIESI NHAKAANVPI IVAINKIDKP TADAQKVRTE LLQHEVFVET
MGGETLEVEV SAKTGQNLDK LLEAILLQAE ILDLKADSER TADGIVIEAK LDQGRGSVAT
VLVQKGTLHL SDIIVAGNEW GRIRALIDDH GNHIKTASPS TPVEILGMQG TPQAGDRFAV
VAHEAKAREI AEYRQRLARD KAAARKTGSR SSLEQMMTKL QTVGVKEFSL IIKGDVQGSI
EAITAALEKL GNEEVQTRIV HSGAGGITES DISLAETSNS VVIGFNVRAN KQVRDLAETQ
GIEIRYYNII YDLVDDIKAA MSGLLSPEKR ETFLGNAEIL EIFNITKIGK VAGCQVTEGK
IERGAGVRLI RDNIVIHEGK LKTLKRFKDE VNEVQIGQEC GIAFEKYEDM RAGDTIEIFR
VEHVNRTL
