IF2_CHLFF
ID IF2_CHLFF Reviewed; 881 AA.
AC Q254H4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CF0542;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
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; AP006861; BAE81314.1; -; Genomic_DNA.
DR AlphaFoldDB; Q254H4; -.
DR SMR; Q254H4; -.
DR STRING; 264202.CF0542; -.
DR KEGG; cfe:CF0542; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_3_2_0; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001260; 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.
FT CHAIN 1..881
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008224"
FT DOMAIN 387..556
FT /note="tr-type G"
FT REGION 31..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..403
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 421..425
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 496..499
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 532..534
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 46..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 396..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 442..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 496..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 881 AA; 96155 MW; 26C4D79BD9A8B422 CRC64;
MEKAKLTKNL KLKIKNAQLT KAAGLDKLKQ KLAQAGSSDT KNSSEKPSAK VAEKVVKKKS
VVDPSVSATP ESVSSETSPR RIRAKNRSSF VSEDLEVSSP VPVDSDTTSS MPPVEEEIAS
STDSEPEVIE VTQPPIEEKS EVVTKVPPTP LKEPEVVVKK DPPKSVVGIK SNFGPTGKHI
NHLLAKTFKA PKKEDKPAPK ERSGQAQAKP QQSSEASSEN KPHSPNNNRS SQPFYRRDTS
KKPGSDFRDR AKKDDNPKAF TGRDRYGLND GSDDDKWRKK RVQKTKKHYD EHTIQRPTHI
KVPLPITIKD LAAEMKLKAS ELIQKMFIHG MTYVVNDVLD NETTVQFIGL EFGCTIDIDS
SEQDKLCIES NTVKEEIQET DPSKLIIRPP IVAFMGHVDH GKTTLIDSLR KSNIAAVEAG
AITQHMGAFC CSTPVGNITI LDTPGHEAFS AMRARGAEVC DIVVLVVAGD EGIKEQTLEA
VKHARAANIT IVVAINKCDK PNFNAETIYR QLSEINLLPE AWGGTTVTVN TSAKTGEGLP
ELLEMLALQA EVLELKANPS ARARGIVIES ELHKGLGAVA TILVQNGTLH LGEALVFNDC
YGKVKTMHDE HNRLMKVASP SVPALITGLS SMPKAGDPFV VVKNEKIAKD IIGARLAGQQ
KFALQKKRPN FDAMLQNKKI LKLIIKADVQ GSIEALASSI LKIVSDKVSA EILSNSVGEI
SESDIRLAAA SKAVIIGFHT GIESHAESLI KSLGVKVQLF NIIYHAVDAV KEMMTALLDP
IAEEKNLGSA EIKETFKSSQ LGTIYGCLVS EGVMTRNQKV RVVRNNDVLW KGTLSSLKRI
KEDVKEVKKG LECGILLEGY QNAQVGDILQ CYEVIYHPQK L
