IF2_PARUW
ID IF2_PARUW Reviewed; 920 AA.
AC Q6MD64;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=pc0761;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(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; BX908798; CAF23485.1; -; Genomic_DNA.
DR RefSeq; WP_011175311.1; NC_005861.1.
DR AlphaFoldDB; Q6MD64; -.
DR SMR; Q6MD64; -.
DR STRING; 264201.pc0761; -.
DR PRIDE; Q6MD64; -.
DR EnsemblBacteria; CAF23485; CAF23485; PC_RS03655.
DR KEGG; pcu:PC_RS03655; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_3_0_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000529; 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; 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..920
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228221"
FT DOMAIN 418..585
FT /note="tr-type G"
FT REGION 27..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..434
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 452..456
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 473..476
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 527..530
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 563..565
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 48..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 473..477
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 527..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 920 AA; 101783 MW; 67B581DDB0A94631 CRC64;
MAKNLKLNIK NAQIAEAINL SGLKSKLAKK KEEESTQKSS AAKSTSKTTK TEVEELPKEE
APRIRARSKS AFAEAPADQS SKEITEEIKT SQDEESISRE AAKVIEEKSR MKTSAEIRQE
IFGEELSQAP SKDSSQELEF AEKIKTNETK PTTFIEPTIA SPAPAEPKSL VEDKTSITHV
YQNQKRDIPI RESLPPQEKL GPTGKHMRDF IKPKPQPERV SRPLEANNSN QKEVSEANKE
KLDKNKIKPK SKGFEEPKVL TADDDARKGL KSPKFKEFKD IKPARKPETR QFDARDRQGL
RTSDEDQHWR KKKNKQRQNI QEDTTIRPTS LKVRLPISIK DLASEMKLKA SQLVGKLFLQ
GIVVTLNDLL EDETTAQLLG QEFGCEITID TAEEKRIQIT DKSIREELQQ SPTDQLQLRP
PVVAFMGHVD HGKTSLIDAI RKSNRAAGEA GAITQHIGAF RCHTTVGDIA ILDTPGHEAF
SAMRARGADV TDIVVLVVAG DEGLRQQSIE AIQHARAANV IIVVAINKCD KPNFNPDNVY
RQLAEQNLLP EPWGGQTITV NCSAVTGEGI PELLEMLALQ AEVLELRANP SMRARGTVLE
SEMHKGLGSV ATILVQNGTL KRGDALVFGL LWGRVKTMHD EYGKELQEAG PSTPVEITGL
SGLPEAGQEF IVVKNEKEAR EIANVRSEGA RQNTFMLQQK KKVSMENMLQ QASATGKKML
NIVLRADVQG SLEALKVALL KIESDKADLN IIFNGVGEVS ESDVQLAAAS KAIVLGFHTQ
IESHAEALVK QLGVQVRLHN IIYHAIDDIK VLMAGLLEKI AQETEKGKAI VKATFKSSQA
GIIAGCQVIE GSIHRNNYVR LKRGQEVIWK GTISSLKRVK EDVREVQKGI ECGILLNNFT
DILEGDIIEA YDITYISQEL
