ID A0A0T9XA48_SALET Unreviewed; 892 AA.
AC A0A0T9XA48;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:SUE45877.1};
GN ORFNames=B7N00_19580 {ECO:0000313|EMBL:EDG5019152.1}, B7N01_16585
GN {ECO:0000313|EMBL:EDG4996040.1}, B7N35_18305
GN {ECO:0000313|EMBL:EDG5127981.1}, B7N72_14925
GN {ECO:0000313|EMBL:EDG5371397.1}, B7N78_00545
GN {ECO:0000313|EMBL:EDG5278283.1}, B7N80_14395
GN {ECO:0000313|EMBL:EDG5289571.1}, B7N84_04160
GN {ECO:0000313|EMBL:EDG5265543.1}, DRU31_15065
GN {ECO:0000313|EMBL:EBS2453613.1}, E0916_17860
GN {ECO:0000313|EMBL:ECF1447813.1}, EJV93_00330
GN {ECO:0000313|EMBL:ECA2719694.1}, ERS008198_02656
GN {ECO:0000313|EMBL:CNU38910.1}, ERS008202_01964
GN {ECO:0000313|EMBL:CNU12806.1}, ERS008207_03962
GN {ECO:0000313|EMBL:CNU97945.1}, EWC73_18625
GN {ECO:0000313|EMBL:ECE8538199.1}, G0B02_20010
GN {ECO:0000313|EMBL:HAC6381358.1}, G0D18_18185
GN {ECO:0000313|EMBL:HAC6682544.1}, G2206_16870
GN {ECO:0000313|EMBL:HAE0436421.1}, NCTC5754_00673
GN {ECO:0000313|EMBL:SUE45877.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE45877.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|Proteomes:UP000039541, ECO:0000313|Proteomes:UP000041314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3476 {ECO:0000313|EMBL:CNU12806.1,
RC ECO:0000313|Proteomes:UP000039541}, A1104
RC {ECO:0000313|EMBL:CNU38910.1, ECO:0000313|Proteomes:UP000041314}, and
RC D4891 {ECO:0000313|EMBL:CNU97945.1,
RC ECO:0000313|Proteomes:UP000042394};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6381358.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381358.1}, M123
RC {ECO:0000313|EMBL:HAC6682544.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0436421.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE45877.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE45877.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EBS2453613.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4996040.1}, 138330
RC {ECO:0000313|EMBL:EDG5289571.1}, 143652
RC {ECO:0000313|EMBL:EDG5371397.1}, 273631
RC {ECO:0000313|EMBL:EDG5019152.1}, 330535
RC {ECO:0000313|EMBL:EDG5265543.1}, 333944
RC {ECO:0000313|EMBL:EDG5278283.1}, 337042
RC {ECO:0000313|EMBL:EDG5127981.1}, 387147
RC {ECO:0000313|EMBL:EBS2453613.1}, 470200
RC {ECO:0000313|EMBL:ECE8538199.1}, 598023
RC {ECO:0000313|EMBL:ECA2719694.1}, and 692616
RC {ECO:0000313|EMBL:ECF1447813.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAC6381358.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381358.1}, M123
RC {ECO:0000313|EMBL:HAC6682544.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0436421.1};
RG NCBI Pathogen Detection Project;
RL Submitted (AUG-2018) 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|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; CQPC01000021; CNU12806.1; -; Genomic_DNA.
DR EMBL; CQPA01000020; CNU38910.1; -; Genomic_DNA.
DR EMBL; CQPD01000050; CNU97945.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000011; EBS2453613.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000001; ECA2719694.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000020; ECE8538199.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000013; ECF1447813.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000018; EDG4996040.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000017; EDG5019152.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000018; EDG5127981.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000002; EDG5265543.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000001; EDG5278283.1; -; Genomic_DNA.
DR EMBL; AAMEML010000015; EDG5289571.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000016; EDG5371397.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000017; HAC6381358.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000016; HAC6682544.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000019; HAE0436421.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE45877.1; -; Genomic_DNA.
DR RefSeq; WP_000133064.1; NZ_WFIN01000002.1.
DR AlphaFoldDB; A0A0T9XA48; -.
DR SMR; A0A0T9XA48; -.
DR Proteomes; UP000039541; Unassembled WGS sequence.
DR Proteomes; UP000041314; Unassembled WGS sequence.
DR Proteomes; UP000042394; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 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; SSF46955; Putative DNA-binding domain; 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}.
FT DOMAIN 391..560
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 88..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..542
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 88..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 446..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 500..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 892 AA; 97402 MW; 0D690F8E64505885 CRC64;
MTDVTLKALA AERQVSVDRL VQQFADAGIR KSADDSVSAQ EKQTLLAHLN REAVSGPDKL
TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR TFVKRDPQEA ERLAAEEQAQ REAEEQARRE
AEEQAKREAQ QKAEREAAEQ AKREAAEKAK REAAEKDKVS NQQTDDMTKT AQAEKARREN
EAAELKRKAE EEARRKLEEE ARRVAEEARR MAEENKWTAT PEPVEDTSDY HVTTSQHARQ
AEDENDREVE GGRGRGRNAK AARPAKKGKH AESKADREEA RAAVRGGKGG KRKGSSLQQG
FQKPAQAVNR DVVIGETITV GELANKMAVK GSQVIKAMMK LGAMATINQV IDQETAQLVA
EEMGHKVILR RENELEEAVM SDRDTGAAAE PRAPVVTIMG HVDHGKTSLL DYIRSTKVAS
GEAGGITQHI GAYHVETDNG MITFLDTPGH AAFTSMRARG AQATDIVVLV VAADDGVMPQ
TIEAIQHAKA AGVPVVVAVN KIDKPEADPD RVKNELSQYG ILPEEWGGES QFVHVSAKAG
TGIDELLDAI LLQAEVLELK AVRKGMASGA VIESFLDKGR GPVATVLVRE GTLHKGDIVL
CGFEYGRVRA MRNELGQEVL EAGPSIPVEI LGLSGVPAAG DEVTVVRDEK KAREVALYRQ
GKFREVKLAR QQKSKLENMF ANMTEGEVHE VNIVLKADVQ GSVEAISDSL LKLSTDEVKV
KIIGSGVGGI TETDATLAAA SNAILVGFNV RADASARKVI ESESLDLRYY SVIYNLIDEV
KAAMSGMLSP ELKQQIIGLA EVRDVFKSPK FGAIAGCMVT EGTIKRHNPI RVLRDNVVIY
EGELESLRRF KDDVNEVRNG MECGIGVKNY NDVRVGDMIE VFEIIEIQRT IA
//
