ID A0A135W526_9BACL Unreviewed; 808 AA.
AC A0A135W526;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AU377_11140 {ECO:0000313|EMBL:KXH80021.1};
OS Sporosarcina sp. HYO08.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1759557 {ECO:0000313|EMBL:KXH80021.1, ECO:0000313|Proteomes:UP000070230};
RN [1] {ECO:0000313|EMBL:KXH80021.1, ECO:0000313|Proteomes:UP000070230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYO08 {ECO:0000313|EMBL:KXH80021.1,
RC ECO:0000313|Proteomes:UP000070230};
RA Choi I.-G., Park W.;
RT "Draft genome sequences of microorganisms having biocementation activity.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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: 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:KXH80021.1}.
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DR EMBL; LPUT01000028; KXH80021.1; -; Genomic_DNA.
DR RefSeq; WP_067408192.1; NZ_LPUT01000028.1.
DR AlphaFoldDB; A0A135W526; -.
DR STRING; 1759557.AU377_11140; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000070230; 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; 1.10.10.2480; -; 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; 2.
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|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:UP000070230}.
FT DOMAIN 310..479
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..461
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 72..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 365..369
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 419..422
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 808 AA; 87658 MW; 6D022D672DAD1A85 CRC64;
MTKIRVHEYA KRVNRTSKEV IEELGKINVS VTNHMSTLDH EAISKLDRKF SKQSAPKAET
NNRGRQDAPK SERPAGNTSS ENRPNQPRSR QGGQSTNRPV NSGQNRPGQG NQQRSGGGAQ
GGNRPGQGNQ QRSGGGSQGN NRPAATSGGQ NRPGQGNQQR PGGGSQGGNR PAATSGGQNR
PNSRPGGGNP NRSGGRGGRP PARGINQGRR RYRPEPQPKV EQPLPEKITF YESLSVGELA
QKLHREPSEI IKKLFMLGVM ATINQELDKD AIELICADYG VEVEEEIRID VTDLEIYFEE
SEEIEAGNTE RPPVVTIMGH VDHGKTTLLD SIRNTKVTQG EAGGITQHIG AYQITEGDKK
ITFLDTPGHA AFTTMRARGA KVTDITILVV AADDGVMPQT VEAINHAKAA EVPIIVAVNK
MDKPTANPDR VMQELTEHGL VAEAWGGDAI FVPISALKGE GIDQLLEMVL LVAEVGELKA
NPSIRARGTV IEAELDRGRG AVATLLVQDG TLHVGDPIVV GNTFGRVRAM INDIGRRVKD
AGPSTPVEIT GLSNVPQAGD RFVVFEDEKT ARQIGESRAM EALQEQRGEK TRVTLDNLFD
QMKQGEMKEL NLIVKADVQG TVEAMAASLM KIEVEGVNVK IIHTGAGAIN ESDISLAAAS
NAIVIGFNVR PDVNARRAAE EEGVDIRLHR VIYKMIEEIE SAMKGMLDPE YEEKVIGQVE
VRETFKVSKI GTIAGSYVTE GKITRDSGVR VIRDNIVIFE GELDTLKRFK DDAKEVARGY
ECGITIKNFN DIKEGDVIEA FVMEEIKR
//
