ID A0A1Y2PBM7_9FLAO Unreviewed; 963 AA.
AC A0A1Y2PBM7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=WH52_13115 {ECO:0000313|EMBL:OSY87197.1};
OS Tenacibaculum holothuriorum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1635173 {ECO:0000313|EMBL:OSY87197.1, ECO:0000313|Proteomes:UP000194221};
RN [1] {ECO:0000313|EMBL:OSY87197.1, ECO:0000313|Proteomes:UP000194221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-2 {ECO:0000313|EMBL:OSY87197.1,
RC ECO:0000313|Proteomes:UP000194221};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Tenacibaculum sp. S2-2, isolated from intestinal
RT microbiota of sea cucumber, Apostichopus japonicas.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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 -!- 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OSY87197.1}.
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DR EMBL; LAPZ01000014; OSY87197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2PBM7; -.
DR STRING; 1635173.WH52_13115; -.
DR InParanoid; A0A1Y2PBM7; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000194221; Unassembled WGS sequence.
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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {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:UP000194221}.
FT DOMAIN 461..631
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 121..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..111
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 121..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 470..477
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 517..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 571..574
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 963 AA; 106603 MW; 20C91E5A8D07A24A CRC64;
MAEGKKLRLN KVLRELNISL DRAVEHLAKN GYEVEARPTT KISDGEYQVL LDGFQTDKSK
KVASKEVTEE KRKEKEAIRQ QLEAEQEKKR LEEEAKKQEV LKAKAEKLEI KTVGKIDIDS
GKAVEEKAPV VEEKKEEAPV KEEKVTEESK KEVKKEEVVK PVEEKPVVEA KKVEEPKKEE
AQKPKVVKEV KKQPVKPIDV ASKKVEAKKQ PEVKKEKAPE VTAENAEKIK TQYKKLDGPK
ITGQKIDLKQ FERPKKKKPD AKTDNKNADA KKKRKRISKP GAGGNSNAQG NQQGGNRGGQ
NRGGQNQNRG GNRGGQNRGR GRRPVVQKEE LTEAEIQKQV RETLEKLQGK SKKGKGAKYR
RDKRDAHRQQ AEAEMQASQE KVLKVTEFVT VSEIATMMDK PVTEIISACM MLGMMVTMNQ
RLDAETLQIV AEEFNYKVEF VGAEVEESIE EIEDKPEDLE LRAPIVTVMG HVDHGKTSLL
DYVRKANVIA GESGGITQHI GAYGVTLDGG QKIAFLDTPG HEAFTAMRAR GAQVTDIVII
VIATDDDVMP QTKEAISHAQ AAGVPIIFAL NKVDKPNANP DNIRTQLSSM NLLVEEWGGS
FQSQEISAKT GLGIDDLLEK VLLEAEVLEL KANPDKNAVG TVVEAQLDKG RGYVSTILVQ
AGTLKIGDYL LAGKHSGKVR AMFDERGNKV KEAGPSTPVS ILGLDGAPQA GDKFNVFDDE
REAKQIAAKR SQLQREQSVR TQKTLTLDEI GRRIALGDFK ELNIILKGDV DGSVEALTDS
FQKLSTEEIQ VNILHKGVGA ITESDVLLAT ASDAIIVGFN VRPQGNARAV ADREEVDIRT
YSIIYDAIND LKDAMEGMLS PEMKEEVIGN VEIREVYKIS KVGNIAGCMV QSGKITRDAK
VRIIREGIVV HDGELASLKR FKDDVKEVTK GYDCGLQIKN YNDIKEYDTL EVYTEVAVKK
KLK
//
