IF2_LEPBP
ID IF2_LEPBP Reviewed; 917 AA.
AC B0SQH4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LEPBI_I1525;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=456481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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; CP000786; ABZ97632.1; -; Genomic_DNA.
DR RefSeq; WP_012388511.1; NC_010602.1.
DR AlphaFoldDB; B0SQH4; -.
DR SMR; B0SQH4; -.
DR STRING; 456481.LEPBI_I1525; -.
DR KEGG; lbi:LEPBI_I1525; -.
DR HOGENOM; CLU_006301_5_1_12; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 93176at2; -.
DR BioCyc; LBIF456481:LEPBI_RS07505-MON; -.
DR Proteomes; UP000001847; Chromosome I.
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; 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; 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..917
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093799"
FT DOMAIN 414..587
FT /note="tr-type G"
FT REGION 1..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..430
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 448..452
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 469..472
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 523..526
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 559..561
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 39..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 423..430
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 469..473
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 523..526
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 917 AA; 97208 MW; 10065A3CEECEA6C1 CRC64;
MEEQKSIKET LQQGASGDKT KKKLVIKKKA APSDEKKESS PGAQGQTTAT EAKQSSPASS
DKKKDLNELI REEAKRQGLG SGPQAPSQAS PIVSRPDRKP EPLPQPDREK APMDRKPESI
LSGDTSSPNF RSGGGQGGGN QGYFRKEDRN PIVSRPTTPR PPRPEGQTGG GYQGNRGPGQ
GGGYQGNRGP GQGGPGGYQG NRGPGQGGPG GYQGNRGPGQ GGPGGYQGNR GPGQGGPGGY
QGNRGPGQGG PGGYQGNRGA RPIGQGGPGS GRPPGDAPFG APGGLPGAGG PGGAKKRVFD
KEKGGREENE NTKFFKQSFR KQKAQAAALA AVPKEISILE NIQVGEIAKK LNLKPGEVIS
KLMKMGMMVT INNVIDAETA SILADDYGCK VKIVSLYDET VIEEEKDAPE DYITRPPVVT
IMGHVDHGKT KLLDTIRSSR VAEGESGGIT QHIGAYQVET ERGKIAFLDT PGHEAFTSMR
ARGASVTDIV VLVVAADDGV MPQTIEAINH AKEAEVPIIV AVNKIDLPAA NPEKVRQELS
NYGLQPEEWG GTTIFCDISA KSNIGIDKLL EMLIIQAELL DHKANPKRKA KGTIVEAKLD
PGRGAVATVL IQNGTLRVGD AFVAGVHAGR VRAMYDDLGR SIKEAGPSFP ALVTGLDGVP
DAGAPFDVVI DDKEARTISH SRQEYERLGQ SKNAATRVTL DNMSEIIKQG ALKELKVIIK
ADVRGSTEAV KEALEKLSTA DVRLNVIHAG TGAIVDSDII LASASNAIVI GFHTRANPKT
VSLAEKEKVE IKYYSIIYDV VNEVKASMEG MLEPEKVENI IGKVEIRDVF KISKVGNIAG
CMVKSGKVTK QAHVRVISSE TGEITWEGKI KNLKRMKDDV ADVLTGFECG ILLDGFNDFS
VGDEIEAYEI REIARKL
