ID F8L0Z1_PARAV Unreviewed; 913 AA.
AC F8L0Z1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 ECO:0000313|EMBL:CCB86907.1};
GN OrderedLocusNames=PUV_19570 {ECO:0000313|EMBL:CCB86907.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB86907.1, ECO:0000313|Proteomes:UP000000495};
RN [1] {ECO:0000313|EMBL:CCB86907.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
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 ECO:0000256|RuleBase:RU000645}.
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}.
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DR EMBL; FR872580; CCB86907.1; -; Genomic_DNA.
DR RefSeq; WP_006340101.1; NC_015702.1.
DR AlphaFoldDB; F8L0Z1; -.
DR STRING; 765952.PUV_19570; -.
DR KEGG; puv:PUV_19570; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_3_1_0; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000000495; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000000495}.
FT DOMAIN 413..580
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 27..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..564
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 28..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422..429
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 468..472
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 522..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 913 AA; 100012 MW; B80A78D28ACD39AD CRC64;
MAKNLKLTIK NTQIAKAVNL EAVKSKLAAK KNAPESEEQL EAKPVSKPSK KPASEEEVKS
HKEEAAAPRI RARSKSVFAE PGEGKGISEI ASSEDVENQL SEQIEAEETI DEKVAKSSVV
EESIAPIADA ESAKELIEKE EEAVVESLSQ VAEPKIEETV VSVEQEEIIK EAPKPVKEPE
APAPVEAPAP KPAPVREKLG PTGRHIKDLL PPPKPPVAKP KKVEPAAPVR TEADSRDGKP
KPKVKRPTEV ASPEKQEELV QAEKKGPKFK DFRDVKPVKR QPTQMRSFDS RDRQGLREND
EDQNWRKRRG KSARQQEETV TRPTSLSIRL PISLKDLASE MKLKASQLIA KIFLQGIVVT
INDILEDETL VQLLGNEFGC EITIDTTEEE RIRVTDKSIK QEIESTDPSL LRTRPPVVAF
MGHVDHGKTS LIDAIRKSNR AAGEAGAITQ HIGAFCCHTD VGDLTVLDTP GHEAFSSMRA
RGADVTDIVV LVIAGDEGIR QQTVEAIQHA KEAKVTIIVA LNKCDKPNFN AENVYRQLAE
HELLPEAWGG QIITVNCSAT TGEGIKTLLE MLALQTEILE LKANPSARAR GTVLESELHK
GMGSKATILV QNGTLRKGDA LVFEQLWGRI KTIHDEFGRE MDEVPPSTPA EITGLSGLPD
AGQEFIVVSS EKEARSIAEA RMLGIRQVNL QKMKKASLEN VFQQATETAK KVLHVVLRAD
VQGSLEALKV ALEKIKSTKA ELVIISTGVG EIAESDVQLA AASKAVILGF HTKIESHADI
LVKQLGVQVR LHDIIYHAID DIKELMSALL DKIPIETEKG QAEVRAIFKS SHLGIVAGCY
VTDGVIRRND SIRVKRNGQK IWQGPISSLK RVKEDVREVA KGLECGILLN NFGEVQAGDI
LEAFEVTYIS QEL
//
